1sew | pdb_00001sew

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

MEMBRANE CHANNEL STRUCTURE OF HELICOBACTER PYLORI VACUOLATING TOXIN A

spinqualitylabelsall models 1sew Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed Helicobacter pylori is a human pathogen responsible for severe gastric diseases such as peptic ulcers, gastric adenocarcinoma, and gastric lymphoma. Vacuolating toxin (VacA) is crucial in facilitating the colonization of the gastric lining by inducing cell apoptosis and immune suppression. VacA inserts into membranes and forms a hexameric, anion-selective pore. Here we present a structural model of the VacA pore that strongly resembles the structure of an unrelated anion-selective channel, MscS. In our model, Gly residues in GXXXG motifs pack against small Ala or Val side chains to generate the pore. Our model suggests that the same design of two anion-selective channels was achieved by two different evolutionary paths and provides insight into the mechanism of VacA function. Membrane channel structure of Helicobacter pylori vacuolating toxin: role of multiple GXXXG motifs in cylindrical channels.,Kim S, Chamberlain AK, Bowie JU Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5988-91. Epub 2004 Apr 5. PMID:15067113 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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