dc.contributor.author |
Kang, HJ |
en |
dc.contributor.author |
Coulibaly, F |
en |
dc.contributor.author |
Clow, Fiona |
en |
dc.contributor.author |
Proft, Thomas |
en |
dc.contributor.author |
Baker, Edward |
en |
dc.date.accessioned |
2012-02-27T00:19:07Z |
en |
dc.date.issued |
2007 |
en |
dc.identifier.citation |
Science 318(5856):1625-1628 07 Dec 2007 |
en |
dc.identifier.issn |
0036-8075 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/12061 |
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 http://www.sherpa.ac.uk/romeo/issn/0036-8075/ |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
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 |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
72915 |
en |
pubs.org-id |
Medical and Health Sciences |
en |
pubs.org-id |
Medical Sciences |
en |
pubs.org-id |
Molecular Medicine |
en |
pubs.org-id |
Science |
en |
pubs.org-id |
Science Research |
en |
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
en |
pubs.record-created-at-source-date |
2010-09-01 |
en |
pubs.dimensions-id |
18063798 |
en |