Stabilizing isopeptide bonds revealed in Gram-positive bacterial pilus structure

Show simple item record Kang, HJ en Coulibaly, F en Clow, Fiona en Proft, Thomas en Baker, Edward en 2012-02-27T00:19:07Z en 2007 en
dc.identifier.citation Science 318(5856):1625-1628 07 Dec 2007 en
dc.identifier.issn 0036-8075 en
dc.identifier.uri en
dc.description.abstract Many bacterial pathogens have long, slender pili through which they adhere to host cells. The crystal structure of the major pilin subunit from the Gram-positive human pathogen Streptococcus pyogenes at 2.2 angstroms resolution reveals an extended structure comprising two all-beta domains. The molecules associate in columns through the crystal, with each carboxyl terminus adjacent to a conserved lysine of the next molecule. This lysine forms the isopeptide bonds that link the subunits in native pili, validating the relevance of the crystal assembly. Each subunit contains two lysine-asparagine isopeptide bonds generated by an intramolecular reaction, and we find evidence for similar isopeptide bonds in other cell surface proteins of Gram-positive bacteria. The present structure explains the strength and stability of such Gram-positive pili and could facilitate vaccine development. en
dc.publisher American Association for the Advancement of Science en
dc.relation.ispartofseries Science en
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from en
dc.rights.uri en
dc.title Stabilizing isopeptide bonds revealed in Gram-positive bacterial pilus structure en
dc.type Journal Article en
dc.identifier.doi 10.1126/science.1145806 en
pubs.issue 5856 en
pubs.begin-page 1625 en
pubs.volume 318 en
dc.rights.holder Copyright: American Association for the Advancement of Science en
dc.identifier.pmid 18063798 en
pubs.end-page 1628 en
dc.rights.accessrights en
pubs.subtype Article en
pubs.elements-id 72915 en Medical and Health Sciences en Medical Sciences en Molecular Medicine en Science en Science Research en Maurice Wilkins Centre (2010-2014) en
pubs.record-created-at-source-date 2010-09-01 en
pubs.dimensions-id 18063798 en

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