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| | <StructureSection load='2xwx' size='340' side='right' caption='[[2xwx]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='2xwx' size='340' side='right' caption='[[2xwx]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xwx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XWX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XWX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xwx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XWX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XWX FirstGlance]. <br> |
| | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xwx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xwx RCSB], [http://www.ebi.ac.uk/pdbsum/2xwx PDBsum]</span></td></tr> | | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xwx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xwx RCSB], [http://www.ebi.ac.uk/pdbsum/2xwx PDBsum]</span></td></tr> |
| | </table> | | </table> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio cholerae]] | + | [[Category: Bacillo virgola del koch trevisan 1884]] |
| | + | [[Category: Aalten, D M.F van]] |
| | [[Category: Chatterjee, N S]] | | [[Category: Chatterjee, N S]] |
| | [[Category: Eijsink, V G.H]] | | [[Category: Eijsink, V G.H]] |
| | [[Category: Ghosh, A]] | | [[Category: Ghosh, A]] |
| | [[Category: Guerrero, R H]] | | [[Category: Guerrero, R H]] |
| | + | [[Category: Ibrahim, A F.M]] |
| | [[Category: Konarev, P V]] | | [[Category: Konarev, P V]] |
| - | [[Category: Svergun, A F.M Ibrahim D I]] | + | [[Category: Svergun, D I]] |
| | [[Category: Vaaje-Kolstad, G]] | | [[Category: Vaaje-Kolstad, G]] |
| - | [[Category: Vanaalten, D M.F]] | |
| | [[Category: Wong, E]] | | [[Category: Wong, E]] |
| | [[Category: Chitin-binding protein]] | | [[Category: Chitin-binding protein]] |
| Structural highlights
Function
[GBPA_VIBCH] Probably interacts with GlcNAc residues. May promote attachment to both epithelial cell surfaces and chitin. This function enhances bacterial colonization in the gastrointestinal tract and may also be important in the environment by augment colonization of chitinous structures, leading to improved survival. Promotes bacterial attachment to, and colonization of, zooplankton in the aquatic ecosystem.[1]
Publication Abstract from PubMed
Vibrio cholerae is a bacterial pathogen that colonizes the chitinous exoskeleton of zooplankton as well as the human gastrointestinal tract. Colonization of these different niches involves an N-acetylglucosamine binding protein (GbpA) that has been reported to mediate bacterial attachment to both marine chitin and mammalian intestinal mucin through an unknown molecular mechanism. We report structural studies that reveal that GbpA possesses an unusual, elongated, four-domain structure, with domains 1 and 4 showing structural homology to chitin binding domains. A glycan screen revealed that GbpA binds to GlcNAc oligosaccharides. Structure-guided GbpA truncation mutants show that domains 1 and 4 of GbpA interact with chitin in vitro, whereas in vivo complementation studies reveal that domain 1 is also crucial for mucin binding and intestinal colonization. Bacterial binding studies show that domains 2 and 3 bind to the V. cholerae surface. Finally, mouse virulence assays show that only the first three domains of GbpA are required for colonization. These results explain how GbpA provides structural/functional modular interactions between V. cholerae, intestinal epithelium and chitinous exoskeletons.
The Vibrio cholerae colonization factor GbpA possesses a modular structure that governs binding to different host surfaces.,Wong E, Vaaje-Kolstad G, Ghosh A, Hurtado-Guerrero R, Konarev PV, Ibrahim AF, Svergun DI, Eijsink VG, Chatterjee NS, van Aalten DM PLoS Pathog. 2012 Jan;8(1):e1002373. Epub 2012 Jan 12. PMID:22253590[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kirn TJ, Jude BA, Taylor RK. A colonization factor links Vibrio cholerae environmental survival and human infection. Nature. 2005 Dec 8;438(7069):863-6. PMID:16341015 doi:http://dx.doi.org/10.1038/nature04249
- ↑ Wong E, Vaaje-Kolstad G, Ghosh A, Hurtado-Guerrero R, Konarev PV, Ibrahim AF, Svergun DI, Eijsink VG, Chatterjee NS, van Aalten DM. The Vibrio cholerae colonization factor GbpA possesses a modular structure that governs binding to different host surfaces. PLoS Pathog. 2012 Jan;8(1):e1002373. Epub 2012 Jan 12. PMID:22253590 doi:10.1371/journal.ppat.1002373
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