2XWX
Vibrio cholerae colonization factor GbpA crystal structure
Summary for 2XWX
| Entry DOI | 10.2210/pdb2xwx/pdb |
| Descriptor | GLCNAC-BINDING PROTEIN A (2 entities in total) |
| Functional Keywords | chitin-binding protein |
| Biological source | VIBRIO CHOLERAE |
| Cellular location | Secreted : Q9KLD5 |
| Total number of polymer chains | 2 |
| Total formula weight | 86585.97 |
| Authors | Wong, E.,Vaaje-Kolstad, G.,Ghosh, A.,Guerrero, R.H.,Konarev, P.V.,Ibrahim, A.F.M.,Svergun, D.I.,Eijsink, V.G.H.,Chatterjee, N.S.,van Aalten, D.M.F. (deposition date: 2010-11-06, release date: 2011-11-16, Last modification date: 2024-11-13) |
| Primary citation | Wong, E.,Vaaje-Kolstad, G.,Ghosh, A.,Hurtado-Guerrero, R.,Konarev, P.V.,Ibrahim, A.F.M.,Svergun, D.I.,Eijsink, V.G.H.,Chatterjee, N.S.,Van Aalten, D.M.F. The Vibrio Cholerae Colonization Factor Gbpa Possesses a Modular Structure that Governs Binding to Different Host Surfaces. Plos Pathog., 8:2373-, 2012 Cited by PubMed Abstract: 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. PubMed: 22253590DOI: 10.1371/JOURNAL.PPAT.1002373 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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