2qv3

Crystal Structure of the Helicobacter pylori Vacuolating Toxin p55 Domain

spinqualitylabelsall models 2qv3, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2qv3 is a 1 chain structure with sequence from Atcc 43504. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: vacA (ATCC 43504) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VACA2_HELPX] Induces vacuolation of eukaryotic cells. Causes ulceration and gastric lesions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Helicobacter pylori VacA, a pore-forming toxin secreted by an autotransporter pathway, causes multiple alterations in human cells, contributes to the pathogenesis of peptic ulcer disease and gastric cancer, and is a candidate antigen for inclusion in an H. pylori vaccine. Here, we present a 2.4-A crystal structure of the VacA p55 domain, which has an important role in mediating VacA binding to host cells. The structure is predominantly a right-handed parallel beta-helix, a feature that is characteristic of autotransporter passenger domains but unique among known bacterial protein toxins. Notable features of VacA p55 include disruptions in beta-sheet contacts that result in five beta-helix subdomains and a C-terminal domain that contains a disulfide bond. Analysis of VacA protein sequences from unrelated H. pylori strains, including m1 and m2 forms of VacA, allows us to identify structural features of the VacA surface that may be important for interactions with host receptors. Docking of the p55 structure into a 19-A cryo-EM map of a VacA dodecamer allows us to propose a model for how VacA monomers assemble into oligomeric structures capable of membrane channel formation. Crystal structure of the Helicobacter pylori vacuolating toxin p55 domain.,Gangwer KA, Mushrush DJ, Stauff DL, Spiller B, McClain MS, Cover TL, Lacy DB Proc Natl Acad Sci U S A. 2007 Oct 9;104(41):16293-8. Epub 2007 Oct 2. PMID:17911250 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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