2xwx | pdb_00002xwx

Vibrio cholerae colonization factor GbpA crystal structure

spinqualitylabelsall models 2xwx, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xwx is a 2 chain structure with sequence from "bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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