Fet3p

'''Fet3p''' is a multicopper oxidase (MCO)₂ found in ''Saccharomyces cerevisiae'' with a structure consisting of three cupredoxin-like β-barrel domains and four copper ions located in three distinct metal sites (T1 in domain 3, T2, and the binuclear T3 at the interface between domains 1 and 3).<ref>{{cite journal|last=Sedlak|first=E.|author2=Ziegler, L.|author3=Kosman, D. J.|author4=Wittung-Stafshede, P.|title=In vitro unfolding of yeast multicopper oxidase Fet3p variants reveals unique role of each metal site|journal=Proceedings of the National Academy of Sciences|date=25 November 2008 |volume=105 |issue=49 |pages=19258–19263 |doi=10.1073/pnas.0806431105|pmid=19033465 |pmc=2614749|bibcode=2008PNAS..10519258S|doi-access=free}}</ref><ref>{{cite journal|last=Singh|first=A.|title=Assembly, Activation, and Trafficking of the Fet3p·Ftr1p High Affinity Iron Permease Complex in Saccharomyces cerevisiae|journal=Journal of Biological Chemistry|date=1 March 2006 |volume=281 |issue=19 |pages=13355–13364 |doi=10.1074/jbc.M512042200|pmid=16522632|doi-access=free}}</ref> Fet3p is a type I membrane protein with an orientation that places the amino-terminal oxidase domain in the exocellular space (N_exo) and the carboxyl terminus in the cytoplasm (C_cyt).

Part of the ferroxidase reaction, Fet3p catalyzes the oxidation of Fe(II) to Fe(III) using O₂ as substrate. The Fe(III) generated by Fet3p is a ligand for the iron permease, Ftr1p.

==References== {{reflist}}

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Category:Oxidoreductases