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dc.contributor.authorBann, James G.
dc.contributor.authorPinkner, Jerome S.
dc.contributor.authorFrieden, Carl
dc.contributor.authorHultgren, Scott J.
dc.date.accessioned2019-04-17T17:24:27Z
dc.date.available2019-04-17T17:24:27Z
dc.date.issued2004-12-14
dc.identifier.citation"Bann, J.G., Pinkner, J.S., Frieden, C., Hultgren, S.J. Catalysis of protein folding by chaperones in pathogenic bacteria (2004) Proceedings of the National Academy of Sciences of the United States of America, 101 (50), pp. 17389-17393. Cited 36 times."
dc.identifier.isbn
dc.identifier.issn0027-8424
dc.identifier.urihttp://dx.doi.org/10.1073/pnas.0408072101
dc.identifier.urihttp://hdl.handle.net/10057/16019
dc.descriptionClick on the DOI link below to access the article (may not be free).
dc.description.abstractMolecular chaperones are thought to inhibit off-pathway interactions such as aggregation from occurring without influencing the on-pathway formation of native structure. Here, we present a mechanism whereby the family of PapD-like chaperones, which are involved in the formation of adhesive pili in pathogenic bacteria, function by suppressing aggregation while simultaneously catalyzing the folding of subunits that make up the pilus. We also show that the Arg-8 residue, invariant in the cleft of all known PapD-like chaperones, makes up part of the active site of the chaperone. The data argue for a temporal mechanism of catalyzed folding. The terminal carboxylate group of a pilus subunit anchors to the active site of the chaperone by hydrogen bonding. This bonding spatially fixes the COOH terminus of the subunit in the correct context for β-sheet formation, using the edge of the NH2-terminal domain of the chaperone as a nucleation site.
dc.language.isoen-US
dc.relation.ispartofseriesNational Academy of Sciences. Proceedings
dc.relation.ispartofseriesv 101, no 50
dc.subjectAggregation||Complex||PapD||PapD-papE||PapE
dc.titleCatalysis of protein folding by chaperones in pathogenic bacteria
dc.typeArticle
dc.rights.holderCopyright Elsevier B.V.


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