dc.contributor.author |
Kang, HJ |
en |
dc.contributor.author |
Paterson, Neil |
en |
dc.contributor.author |
Gaspar, AH |
en |
dc.contributor.author |
Ton-That, H |
en |
dc.contributor.author |
Baker, Edward |
en |
dc.date.accessioned |
2012-02-27T00:06:10Z |
en |
dc.date.issued |
2009 |
en |
dc.identifier.citation |
Proc Natl Acad Sci U S A 106(40):16967-16971 06 Oct 2009 |
en |
dc.identifier.issn |
0027-8424 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/12055 |
en |
dc.description.abstract |
Cell-surface pili are important virulence factors that enable bacterial pathogens to adhere to specific host tissues and modulate host immune response. Relatively little is known about the structure of Gram-positive bacterial pili, which are built by the sortase-catalyzed covalent crosslinking of individual pilin proteins. Here we report the 1.6-Å resolution crystal structure of the shaft pilin component SpaA from Corynebacterium diphtheriae, revealing both common and unique features. The SpaA pilin comprises 3 tandem Ig-like domains, with characteristic folds related to those typically found in non-pilus adhesins. Whereas both the middle and the C-terminal domains contain an intramolecular Lys–Asn isopeptide bond, previously detected in the shaft pilins of Streptococcus pyogenes and Bacillus cereus, the middle Ig-like domain also harbors a calcium ion, and the C-terminal domain contains a disulfide bond. By mass spectrometry, we show that the SpaA monomers are cross-linked in the assembled pili by a Lys–Thr isopeptide bond, as predicted by previous genetic studies. Together, our results reveal that despite profound dissimilarities in primary sequences, the shaft pilins of Gram-positive pathogens have strikingly similar tertiary structures, suggesting a modular backbone construction, including stabilizing intermolecular and intramolecular isopeptide bonds. |
en |
dc.publisher |
National Academy of Sciences |
en |
dc.relation.ispartofseries |
Proceedings of the National Academy of Sciences of the United States of America |
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/1091-6490/ |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.title |
The Corynebacterium diphtheriae shaft pilin SpaA is built of tandem Ig-like modules with stabilizing isopeptide and disulfide bonds |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1073/pnas.0906826106 |
en |
pubs.issue |
40 |
en |
pubs.begin-page |
16967 |
en |
pubs.volume |
106 |
en |
dc.rights.holder |
Copyright: National Academy of Sciences |
en |
dc.identifier.pmid |
19805181 |
en |
pubs.author-url |
http://www.pnas.org/cgi/content/full/0906826106/DCSupplemental |
en |
pubs.end-page |
16971 |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
89198 |
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 |
19805181 |
en |