Autochaperone

In molecular biology, autotransporter proteins are proteins secreted out the Gram-negative bacteria. These beta helixes require a domain which is called the intramolecular '''autochaperone domain'''. It shows similarities with other intramolecular chaperone sequences and has a folding-associated function. This increases the efficiency, either by stabilizing the beta-barrel, or by promoting the folding of the passenger domain.

The autochaperone domain is usually located between the HSF and the passenger domain. When the passenger domain is translocated, starting with its C terminus, the autochaperone domain is first out. This would result in the formation of a hairpin structure.

==References== {{reflist}}

==External links== * [https://web.archive.org/web/20110807092431/http://www.doaj.org/doaj?func=abstract&id=175033] Surface display of proteins by Gram-negative bacterial autotransporters * [https://archive.today/20130202011722/http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6VN3-4J9MWS9-1&_user=499882&_coverDate=06/30/2006&_rdoc=1&_fmt=high&_orig=search&_origin=search&_sort=d&_docanchor=&view=c&_searchStrId=1470198162&_rerunOrigin=scholar.google&_acct=C000024498&_version=1&_urlVersion=0&_userid=499882&md5=2c1a1e0d466b5eb2c0955b5397c4402c&searchtype=a] Adhesion mediated by autotransporters of Gram-negative bacteria: Structural and functional features * [http://jb.asm.org/cgi/content/abstract/185/2/489] Identification of Secretion Determinants of the Bordetella pertussis BrkA Autotransporter

{{DEFAULTSORT:Autochaperone}} Category:Protein structural motifs Category:Protein domains