{{Short description|Type of beta barrel protein domain structure}} [[File:4oq9 chainA jellyroll.png|thumb|right|A canonical example of a jelly roll viral capsid protein, from the [[satellite tobacco mosaic virus]]. The individual [[beta strand]]s are labeled with their traditional designations (for historical reasons, sheet A is not used), highlighting the packing of the BIDG and CHEF four-stranded sheets.<ref name="larson_2014">{{cite journal | vauthors = Larson SB, Day JS, McPherson A | title = Satellite tobacco mosaic virus refined to 1.4 Å resolution | journal = Acta Crystallographica. Section D, Biological Crystallography | volume = 70 | issue = Pt 9 | pages = 2316–30 | date = September 2014 | pmid = 25195746 | pmc = 4157444 | doi = 10.1107/S1399004714013789 }}</ref>]] The '''jelly roll''' or '''Swiss roll fold''' is a [[protein fold]] or [[supersecondary structure]] composed of eight [[beta strand]]s arranged in two four-stranded sheets. The name of the structure was introduced by [[Jane S. Richardson]] in 1981, reflecting its resemblance to the jelly or [[Swiss roll]] cake.<ref name="richardson_1981">{{cite book| vauthors = Richardson JS |title=Advances in Protein Chemistry Volume 34|chapter=The anatomy and taxonomy of protein structure|date=1981|volume=34|pages=167–339|doi=10.1016/S0065-3233(08)60520-3|pmid=7020376|isbn=978-0-12-034234-1}}</ref> The fold is an elaboration on the [[Greek key (protein structure)|Greek key motif]] and is sometimes considered a form of [[beta barrel]]. It is very common in [[viral protein]]s, particularly [[viral capsid]] proteins.<ref name="chelvanayagam_1992">{{cite journal | vauthors = Chelvanayagam G, Heringa J, Argos P | title = Anatomy and evolution of proteins displaying the viral capsid jellyroll topology | journal = Journal of Molecular Biology | volume = 228 | issue = 1 | pages = 220–42 | date = November 1992 | pmid = 1447783 | doi = 10.1016/0022-2836(92)90502-B }}</ref><ref name="cheng_2013">{{cite journal | vauthors = Cheng S, Brooks CL | title = Viral capsid proteins are segregated in structural fold space | journal = PLOS Computational Biology | volume = 9 | issue = 2 | article-number = e1002905 | date = 7 February 2013 | pmid = 23408879 | pmc = 3567143 | doi = 10.1371/journal.pcbi.1002905 | bibcode = 2013PLSCB...9E2905C | doi-access = free }}</ref> Taken together, the jelly roll and Greek key structures comprise around 30% of the [[all-beta protein]]s annotated in the [[Structural Classification of Proteins]] (SCOP) database.<ref name="edwards_2013">{{cite journal | vauthors = Edwards H, Abeln S, Deane CM | title = Exploring fold space preferences of new-born and ancient protein superfamilies | journal = PLOS Computational Biology | volume = 9 | issue = 11 | article-number = e1003325 | date = 14 November 2013 | pmid = 24244135 | pmc = 3828129 | doi = 10.1371/journal.pcbi.1003325 | bibcode = 2013PLSCB...9E3325E | doi-access = free }}</ref>
== Structure == The basic jelly roll structure consists of eight [[beta strand]]s arranged in two four-stranded [[antiparallel (biochemistry)|antiparallel]] beta sheets which pack together across a [[hydrophobic]] interface [Where citation... uniprot]. The strands are traditionally labeled B through I for the historical reason that the first solved structure, of a jelly roll capsid protein from the [[tomato bushy stunt virus]], had an additional strand A outside the fold's common core.<ref name="harrison_1978">{{cite journal | vauthors = Harrison SC, Olson AJ, Schutt CE, Winkler FK, Bricogne G | title = Tomato bushy stunt virus at 2.9 A resolution | journal = Nature | volume = 276 | issue = 5686 | pages = 368–73 | date = November 1978 | pmid = 19711552 | doi = 10.1038/276368a0 | bibcode = 1978Natur.276..368H | s2cid = 4341051 }}</ref><ref name="rossmann_1983">{{cite journal | vauthors = Rossmann MG, Abad-Zapatero C, Murthy MR, Liljas L, Jones TA, Strandberg B | title = Structural comparisons of some small spherical plant viruses | journal = Journal of Molecular Biology | volume = 165 | issue = 4 | pages = 711–36 | date = April 1983 | pmid = 6854630 | doi = 10.1016/S0022-2836(83)80276-9 }}</ref> The sheets are composed of strands BIDG and CHEF, folded such that strand B packs opposite strand C, I opposite H, etc.<ref name=cheng_2013 /><ref name=benson_2004 />
==Viral proteins== [[File:4oq9 capsid.png|thumb|right|The full assembled capsid structure of the satellite tobacco mosaic virus, with the monomer shown above at the bottom of the highlighted pentamer. The remainder of the protein chains are shown in purple and the [[RNA]] in the interior of the capsid is shown in brown. The axis of the jelly roll in this single jelly roll capsid is parallel to the capsid surface. From {{PDB|4OQ9}}.<ref name=larson_2014 />]] A large number of [[virus]]es build their exterior [[viral capsid|capsid]]s from proteins containing either a single or a double jelly roll fold. This shared capsid architecture is thought to reflect ancient evolutionary relationships, possibly dating to before the [[last universal common ancestor]] (LUCA) of cellular life.<ref name="benson_2004">{{cite journal | vauthors = Benson SD, Bamford JK, Bamford DH, Burnett RM | title = Does common architecture reveal a viral lineage spanning all three domains of life? | journal = Molecular Cell | volume = 16 | issue = 5 | pages = 673–85 | date = December 2004 | pmid = 15574324 | doi = 10.1016/j.molcel.2004.11.016 | doi-access = free }}</ref><ref name="forterre_2009">{{cite journal | vauthors = Forterre P, Prangishvili D | title = The origin of viruses | journal = Research in Microbiology | volume = 160 | issue = 7 | pages = 466–72 | date = September 2009 | pmid = 19647075 | doi = 10.1016/j.resmic.2009.07.008 | s2cid = 2767388 }}</ref><ref name="holmes_2011">{{cite journal | vauthors = Holmes EC | title = What does virus evolution tell us about virus origins? | journal = Journal of Virology | volume = 85 | issue = 11 | pages = 5247–51 | date = June 2011 | pmid = 21450811 | pmc = 3094976 | doi = 10.1128/JVI.02203-10 }}</ref> Other viral lineages use evolutionarily unrelated proteins to build their enclosed capsids, which likely evolved independently at least twice<ref name=forterre_2009 /><ref name=krupovic_2011 /> and possibly many times, with links to proteins of cellular origin.<ref name="krupovic_2017">{{cite journal | vauthors = Krupovic M, Koonin EV | title = Multiple origins of viral capsid proteins from cellular ancestors | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 114 | issue = 12 | pages = E2401–E2410 | date = March 2017 | pmid = 28265094 | doi = 10.1073/pnas.1621061114 | pmc = 5373398 | bibcode = 2017PNAS..114E2401K | doi-access = free }}</ref>
===Single jelly roll capsid proteins=== Single jelly roll capsid (JRC) proteins are found in at least sixteen distinct viral [[Family (taxonomy)|families]], mostly with [[icosahedral]] capsid structures and including both [[RNA virus]]es and [[DNA virus]]es.<ref>{{cite journal | vauthors = Krupovic M | title = Networks of evolutionary interactions underlying the polyphyletic origin of ssDNA viruses | journal = Current Opinion in Virology | volume = 3 | issue = 5 | pages = 578–86 | date = October 2013 | pmid = 23850154 | doi = 10.1016/j.coviro.2013.06.010 }}</ref> Many viruses with single jelly roll capsids are [[positive-sense single-stranded RNA virus]]es. Two groups of [[double-stranded DNA virus]]es with single-JRC capsids are the ''[[Papillomaviridae]]'' and ''[[Polyomaviridae]]'', both of which have fairly small capsids; in these viruses, the architecture of the assembled capsid orients the axis of the jelly roll parallel or "horizontally" relative to the capsid surface.<ref name="krupovic_2011">{{cite journal | vauthors = Krupovic M, Bamford DH | title = Double-stranded DNA viruses: 20 families and only five different architectural principles for virion assembly | journal = Current Opinion in Virology | volume = 1 | issue = 2 | pages = 118–24 | date = August 2011 | pmid = 22440622 | doi = 10.1016/j.coviro.2011.06.001 }}</ref> A large-scale analysis of viral capsid components suggested that the single horizontal jelly roll is the most common fold among capsid proteins, accounting for about 28% of known examples.<ref name=krupovic_2017 />
Another group of viruses uses single jelly roll proteins in their capsids, but in the vertical rather than horizontal orientation. These viruses are evolutionarily related to the large group of double jelly-roll viruses known as the [[PRD1]]-[[adenovirus]] viral lineage, with similar capsid architecture realized through assembly of two distinct single jelly-roll major capsid proteins expressed from distinct genes.<ref name="gil-carton_2015">{{cite journal | vauthors = Gil-Carton D, Jaakkola ST, Charro D, Peralta B, Castaño-Díez D, Oksanen HM, Bamford DH, Abrescia NG | display-authors = 6 | title = Insight into the Assembly of Viruses with Vertical Single β-barrel Major Capsid Proteins | journal = Structure | volume = 23 | issue = 10 | pages = 1866–1877 | date = October 2015 | pmid = 26320579 | doi = 10.1016/j.str.2015.07.015 | doi-access = free }}</ref><ref name="santos-perez_2019">{{cite journal | vauthors = Santos-Pérez I, Charro D, Gil-Carton D, Azkargorta M, Elortza F, Bamford DH, Oksanen HM, Abrescia NG | display-authors = 6 | title = Structural basis for assembly of vertical single β-barrel viruses | journal = Nature Communications | volume = 10 | issue = 1 | page = 1184 | date = March 2019 | pmid = 30862777 | doi = 10.1038/s41467-019-08927-2 | pmc = 6414509 | bibcode = 2019NatCo..10.1184S }}</ref> These single vertical jelly-roll viruses comprise the taxon [[Helvetiavirae]].<ref name=koonin_2019 /> Known viruses with vertical single jelly roll capsids infect [[extremophilic]] [[prokaryote]]s.<ref name=gil-carton_2015 /><ref name=krupovic_2017 />
===Double jelly roll proteins=== [[File:2w0c_monomer.png|thumb|right|A monomer of the double jelly roll major capsid protein P2 from [[bacteriophage PM2]]. The two distinct jelly roll domains are shown in red and blue, with the remaining protein sequence in orange. Double jelly rolls are oriented with the "vertical" axis perpendicular to the capsid surface, which is at the bottom in this image. From {{PDB|2W0C}}.<ref name="abrescia_2008">{{cite journal | vauthors = Abrescia NG, Grimes JM, Kivelä HM, Assenberg R, Sutton GC, Butcher SJ, Bamford JK, Bamford DH, Stuart DI | display-authors = 6 | title = Insights into virus evolution and membrane biogenesis from the structure of the marine lipid-containing bacteriophage PM2 | journal = Molecular Cell | volume = 31 | issue = 5 | pages = 749–61 | date = September 2008 | pmid = 18775333 | doi = 10.1016/j.molcel.2008.06.026 | doi-access = free }}</ref>]] [[File:2w0c_trimer.png|thumb|right|A pseudohexameric trimer of double jelly roll proteins; the jelly rolls are in red and blue and the loops and helices are colored to distinguish the three monomers in the assembly. The viewer is looking down from the exterior toward the capsid surface. From {{PDB|2W0C}}.<ref name=abrescia_2008 />]] Double jelly roll capsid proteins consist of two single jelly roll folds connected by a short linker region. They are found in both [[double-stranded DNA virus]]es and [[single-stranded DNA viruses]] of at least ten different viral families, including viruses that infect all [[domains of life]], and spanning a large capsid size range.<ref name=cheng_2013 /><ref name=krupovic_2011 /><ref>{{cite journal | vauthors = Laanto E, Mäntynen S, De Colibus L, Marjakangas J, Gillum A, Stuart DI, Ravantti JJ, Huiskonen JT, Sundberg LR | display-authors = 6 | title = Virus found in a boreal lake links ssDNA and dsDNA viruses | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 114 | issue = 31 | pages = 8378–8383 | date = August 2017 | pmid = 28716906 | pmc = 5547622 | doi = 10.1073/pnas.1703834114 | bibcode = 2017PNAS..114.8378L | doi-access = free }}</ref> In the double jelly roll capsid architecture, the jelly roll axis is oriented perpendicular or "vertically" relative to the capsid surface.<ref name="krupovic_2008">{{cite journal | vauthors = Krupovic M, Bamford DH | title = Virus evolution: how far does the double beta-barrel viral lineage extend? | journal = Nature Reviews. Microbiology | volume = 6 | issue = 12 | pages = 941–8 | date = December 2008 | pmid = 19008892 | doi = 10.1038/nrmicro2033 | s2cid = 31542714 }}</ref>
Double jelly roll proteins are believed to have evolved from single jelly roll proteins by [[gene duplication]].<ref name=krupovic_2011 /><ref name="krupovic_2008" /> It is likely that vertical single jelly roll viruses represent a transitional form, and that the vertical and horizontal jelly roll capsid proteins have independent evolutionary origins from ancestral cellular proteins.<ref name=krupovic_2017 /> The degree of structural similarity among double-jelly-roll virus capsids has led to the conclusion that these viruses likely have a common evolutionary origin despite their diversity in size and in host range; this has become known as the [[PRD1]]-[[adenovirus]] lineage ([[Bamfordvirae]]).<ref name=krupovic_2008 /><ref name=koonin_2019>{{cite journal |title=Create a megataxonomic framework, filling all principal taxonomic ranks, for DNA viruses encoding vertical jelly roll-type major capsid proteins |vauthors=Koonin EV, Dolja VV, Krupovic M, Varsani A, Wolf YI, Yutin N, Zerbini M, Kuhn JH|journal=ICTV Proposal (Taxoprop) |date=October 2019 |page=2019.003G |doi=10.13140/RG.2.2.14886.47684 |url=https://www.researchgate.net/publication/339913931}}</ref><ref name="koonin_2020">{{cite journal | vauthors = Koonin EV, Dolja VV, Krupovic M, Varsani A, Wolf YI, Yutin N, Zerbini FM, Kuhn JH | display-authors = 6 | title = Global Organization and Proposed Megataxonomy of the Virus World | journal = Microbiology and Molecular Biology Reviews | volume = 84 | issue = 2 | pages = e00061–19, /mmbr/84/2/MMBR.00061–19.atom | date = May 2020 | pmid = 32132243 | doi = 10.1128/MMBR.00061-19 | pmc = 7062200 }}</ref><ref name="walker_2020">{{cite journal | vauthors = Walker PJ, Siddell SG, Lefkowitz EJ, Mushegian AR, Adriaenssens EM, Dempsey DM, Dutilh BE, Harrach B, Harrison RL, Hendrickson RC, Junglen S, Knowles NJ, Kropinski AM, Krupovic M, Kuhn JH, Nibert M, Orton RJ, Rubino L, Sabanadzovic S, Simmonds P, Smith DB, Varsani A, Zerbini FM, Davison AJ | display-authors = 6 | title = Changes to virus taxonomy and the Statutes ratified by the International Committee on Taxonomy of Viruses (2020) | journal = Archives of Virology | volume = 165 | issue = 11 | pages = 2737–2748 | date = November 2020 | pmid = 32816125 | doi = 10.1007/s00705-020-04752-x | s2cid = 221182789 | doi-access = free | url = https://dspace.library.uu.nl/bitstream/handle/1874/409146/Changes.pdf?sequence=1&isAllowed=y }}</ref> Many members of this group have been identified through [[metagenomics]] and in some cases have few to no other viral genes in common.<ref name=krupovic_2017 /><ref name="yutin_2018">{{cite journal | vauthors = Yutin N, Bäckström D, Ettema TJ, Krupovic M, Koonin EV | title = Vast diversity of prokaryotic virus genomes encoding double jelly-roll major capsid proteins uncovered by genomic and metagenomic sequence analysis | journal = Virology Journal | volume = 15 | issue = 1 | page = 67 | date = April 2018 | pmid = 29636073 | doi = 10.1186/s12985-018-0974-y | pmc = 5894146 | doi-access = free }}</ref> Although most members of this group have [[Capsid#Icosahedral|icosahedral]] capsid geometry, a few families such as the ''[[Poxviridae]]'' and ''[[Ascoviridae]]'' have oval or brick-shaped mature virions; poxviruses such as ''[[Vaccinia]]'' undergo dramatic conformational changes mediated by highly derived double jelly roll proteins during maturation and likely derive from an icosahedral ancestor.<ref name=krupovic_2011 /><ref name="bahar_2011">{{cite journal | vauthors = Bahar MW, Graham SC, Stuart DI, Grimes JM | title = Insights into the evolution of a complex virus from the crystal structure of vaccinia virus D13 | journal = Structure | volume = 19 | issue = 7 | pages = 1011–20 | date = July 2011 | pmid = 21742267 | pmc = 3136756 | doi = 10.1016/j.str.2011.03.023 }}</ref> Shared double-jelly-roll capsid proteins, along with other homologous proteins, have also been cited in support of the proposed [[order (biology)|order]] ''[[Megavirales]]'' containing the [[nucleocytoplasmic large DNA virus]]es (NCLDV).<ref name="colson_2013">{{cite journal | vauthors = Colson P, De Lamballerie X, Yutin N, Asgari S, Bigot Y, Bideshi DK, Cheng XW, Federici BA, Van Etten JL, Koonin EV, La Scola B, Raoult D | display-authors = 6 | title = "Megavirales", a proposed new order for eukaryotic nucleocytoplasmic large DNA viruses | journal = Archives of Virology | volume = 158 | issue = 12 | pages = 2517–21 | date = December 2013 | pmid = 23812617 | pmc = 4066373 | doi = 10.1007/s00705-013-1768-6 }}</ref>
Initially, it was believed that double jelly roll proteins are unique to viruses, because they were not observed in cellular proteins.<ref name=krupovic_2011 /> However, in 2022, comparison of protein structures revealed several families of bona fide cellular proteins with the double jelly roll fold <ref name=Krupovic2022PNAS>{{cite journal |last1=Krupovic |first1=M |last2=Makarova |first2=KS |last3=Koonin |first3=EV |title=Cellular homologs of the double jelly-roll major capsid proteins clarify the origins of an ancient virus kingdom. |journal=Proceedings of the National Academy of Sciences of the United States of America |date=1 February 2022 |volume=119 |issue=5 |article-number=e2120620119 |doi=10.1073/pnas.2120620119 |pmid=35078938 |pmc=8812541 |bibcode=2022PNAS..11920620K }}</ref>
===Non-capsid proteins=== Single jelly rolls also occur in non-capsid viral proteins, including minor components of the assembled [[virion]] as well as non-virion proteins such as [[polyhedrin]].<ref name=krupovic_2011 /> In plant viruses, the 30K superfamily [[movement protein]]s responsible for intercellular transport of viral genomes or entire capsids through [[plasmodesmata]] channels have the single jelly-roll fold and have evolved from the capsid proteins of small icosahedral viruses.<ref name=Butkovic2023PlosBiol>{{cite journal |last1=Butkovic |first1=A |last2=Dolja |first2=VV |last3=Koonin |first3=EV |last4=Krupovic |first4=M |title=Plant virus movement proteins originated from jelly-roll capsid proteins. |journal=PLOS Biology |date=2023 |volume=21 |issue=6 |article-number=e3002157 |doi=10.1371/journal.pbio.3002157 |pmid=37319262 |pmc=10306228 |doi-access=free }}</ref>
==Cellular proteins== Both single and double jelly roll folds are found in proteins of cellular origin.<ref name=krupovic_2011 /><ref name=krupovic_2017 /><ref name=Krupovic2022PNAS /> One class of cellular proteins with single jelly roll fold is the [[nucleoplasmin]]s, which serve as [[molecular chaperone]] proteins for [[histone]] assembly into [[nucleosome]]s. The [[N-terminal]] [[protein domain|domain]] of nucleoplasmins possesses a single jelly roll fold and assembled into a pentamer.<ref name="dutta_2001">{{cite journal | vauthors = Dutta S, Akey IV, Dingwall C, Hartman KL, Laue T, Nolte RT, Head JF, Akey CW | display-authors = 6 | title = The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly | journal = Molecular Cell | volume = 8 | issue = 4 | pages = 841–53 | date = October 2001 | pmid = 11684019 | doi = 10.1016/S1097-2765(01)00354-9 | doi-access = free }}</ref> Similar structures have since been reported in additional groups of [[chromatin]] remodeling proteins.<ref name="edlich_2015">{{cite journal | vauthors = Edlich-Muth C, Artero JB, Callow P, Przewloka MR, Watson AA, Zhang W, Glover DM, Debski J, Dadlez M, Round AR, Forsyth VT, Laue ED | display-authors = 6 | title = The pentameric nucleoplasmin fold is present in Drosophila FKBP39 and a large number of chromatin-related proteins | journal = Journal of Molecular Biology | volume = 427 | issue = 10 | pages = 1949–63 | date = May 2015 | pmid = 25813344 | pmc = 4414354 | doi = 10.1016/j.jmb.2015.03.010 }}</ref> Jelly roll motifs with identical beta-sheet connectivity are also found in [[tumor necrosis factor]] ligands<ref name="bodmer_2002">{{cite journal | vauthors = Bodmer JL, Schneider P, Tschopp J | title = The molecular architecture of the TNF superfamily | journal = Trends in Biochemical Sciences | volume = 27 | issue = 1 | pages = 19–26 | date = January 2002 | pmid = 11796220 | doi = 10.1016/S0968-0004(01)01995-8 | url = https://serval.unil.ch/notice/serval:BIB_5073D64C283D }}</ref> and proteins from the bacterium ''[[Yersinia pseudotuberculosis]]'' that belong to a class of viral and bacterial proteins known as [[superantigen]]s.<ref name="donadini_2004">{{cite journal | vauthors = Donadini R, Liew CW, Kwan AH, Mackay JP, Fields BA | title = Crystal and solution structures of a superantigen from Yersinia pseudotuberculosis reveal a jelly-roll fold | journal = Structure | volume = 12 | issue = 1 | pages = 145–56 | date = January 2004 | pmid = 14725774 | doi = 10.1016/j.str.2003.12.002 | doi-access = free }}</ref><ref name="fraser_2008">{{cite journal | vauthors = Fraser JD, Proft T | title = The bacterial superantigen and superantigen-like proteins | journal = Immunological Reviews | volume = 225 | issue = 1 | pages = 226–43 | date = October 2008 | pmid = 18837785 | doi = 10.1111/j.1600-065X.2008.00681.x | s2cid = 39174409 }}</ref>
More broadly, the members of the extremely diverse [[cupin superfamily]] are also often described as jelly rolls; though the common core of the cupin domain structure contains only six beta strands, many cupins have eight.<ref name="khuri_2001">{{cite journal | vauthors = Khuri S, Bakker FT, Dunwell JM | title = Phylogeny, function, and evolution of the cupins, a structurally conserved, functionally diverse superfamily of proteins | journal = Molecular Biology and Evolution | volume = 18 | issue = 4 | pages = 593–605 | date = April 2001 | pmid = 11264412 | doi = 10.1093/oxfordjournals.molbev.a003840 | doi-access = free }}</ref> Examples include the non-[[heme]] [[dioxygenase]] enzymes<ref name="ozer_2007">{{cite journal | vauthors = Ozer A, Bruick RK | title = Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one? | journal = Nature Chemical Biology | volume = 3 | issue = 3 | pages = 144–53 | date = March 2007 | pmid = 17301803 | doi = 10.1038/nchembio863 }}</ref><ref name="aik_2012">{{cite journal | vauthors = Aik W, McDonough MA, Thalhammer A, Chowdhury R, Schofield CJ | title = Role of the jelly-roll fold in substrate binding by 2-oxoglutarate oxygenases | journal = Current Opinion in Structural Biology | volume = 22 | issue = 6 | pages = 691–700 | date = December 2012 | pmid = 23142576 | doi = 10.1016/j.sbi.2012.10.001 }}</ref> (including [[alpha-ketoglutarate-dependent hydroxylases]]) and [[JmjC]]-family [[(Histone-H3)-lysine-36 demethylase|histone demethylases]].<ref name="chen_2006">{{cite journal | vauthors = Chen Z, Zang J, Whetstine J, Hong X, Davrazou F, Kutateladze TG, Simpson M, Mao Q, Pan CH, Dai S, Hagman J, Hansen K, Shi Y, Zhang G | display-authors = 6 | title = Structural insights into histone demethylation by JMJD2 family members | journal = Cell | volume = 125 | issue = 4 | pages = 691–702 | date = May 2006 | pmid = 16677698 | doi = 10.1016/j.cell.2006.04.024 | s2cid = 15273763 | doi-access = free }}</ref><ref name="klose_2007">{{cite journal | vauthors = Klose RJ, Zhang Y | title = Regulation of histone methylation by demethylimination and demethylation | journal = Nature Reviews. Molecular Cell Biology | volume = 8 | issue = 4 | pages = 307–18 | date = April 2007 | pmid = 17342184 | doi = 10.1038/nrm2143 | s2cid = 2616900 }}</ref>
Cellular proteins with the double jelly roll fold include glycoside hydrolases of the DUF2961 family, [[PNGase F|peptide:N-glycosidase F]] (PNGases F) and [[peptidylglycine alpha-amidating monooxygenase]].<ref name=Krupovic2022PNAS /> [[File:Cellular DJRs.png|thumb]] A notable difference between PNGases F and the other double jelly roll proteins is the absence of the α-helices, which follow the F and F' strands in capsid proteins and DUF2961. The equivalent regions are variable in the PNGases F and contain either long loops or insertions. By contrast, jelly-roll domains of DUF2961 proteins contain an insertion of short β-hairpins upstream of the G and G' strands of the double jelly roll fold. Importantly, DUF2961 family proteins form trimers resembling viral capsomers.<ref name=Krupovic2022PNAS />
==Evolution== Comparative studies of proteins classified as jelly roll and [[Greek key (protein structure)|Greek key]] structures suggest that the Greek key proteins evolved significantly earlier than their more topologically complex jelly roll counterparts.<ref name=edwards_2013 /> [[Structural bioinformatics]] studies comparing virus capsid jelly-roll proteins to other proteins of known structure indicates that the capsid proteins form a well-separated cluster, suggesting that they are subject to a distinctive set of evolutionary constraints.<ref name=cheng_2013 /> One of the most notable features of viral capsid jelly roll proteins is their ability to form oligomers in a repeated tiling pattern to produce a closed protein shell; the cellular proteins that are most similar in fold and topology are mostly also oligomers.<ref name=cheng_2013 /> It has been proposed that viral jelly-roll capsid proteins have evolved from cellular jelly-roll proteins, potentially on several independent occasions, at the earliest stages of cellular evolution.<ref name=krupovic_2017 />
==History and nomenclature== The name "jelly roll" was first used for the structure composed of an elaboration on the [[Greek key (protein structure)|Greek key motif]] by [[Jane S. Richardson]] in 1981 and was intended to reflect the structure's resemblance to a jelly or [[Swiss roll]] cake.<ref name=richardson_1981 /> The structure has been given a variety of descriptive names, including a wedge, beta barrel, and beta roll. The edges of the two sheets do not meet to form regular [[hydrogen bond]]ing patterns, and so it is often not considered to be a true [[beta barrel]],<ref name=chelvanayagam_1992 /> though the term is in common use in describing viral capsid architecture.<ref name=gil-carton_2015 /><ref name=santos-perez_2019 /> Cellular proteins containing jelly roll-like structures may be described as a [[cupin]] fold, a [[JmjC]] fold, or a double-stranded beta helix.<ref name=aik_2012 />
== References == {{reflist|30em}}
== External links == * [http://kinemage.biochem.duke.edu/teaching/anatax/html/anatax.3d.html Antiparallel β Domains] {{Webarchive|url=https://web.archive.org/web/20160704160651/http://kinemage.biochem.duke.edu/teaching/anatax/html/anatax.3d.html |date=2016-07-04 }}, a section from ''Anatomy and Taxonomy of Protein Structure'' by Jane S. Richardson * [http://schaechter.asmblog.org/schaechter/2014/05/the-jelly-roll-of-life.html The Jelly Roll of Life] by Jacqueline Humphries at ''Small Things Considered'', a blog sponsored by the [[American Society for Microbiology]]
[[Category:Protein folds]]