2qv3

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[[Image:2qv3.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_2qv3", creates the "Structure Box" on the page.
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|GENE= vacA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori])
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{{STRUCTURE_2qv3| PDB=2qv3 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qv3 OCA], [http://www.ebi.ac.uk/pdbsum/2qv3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qv3 RCSB]</span>
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'''Crystal Structure of the Helicobacter pylori Vacuolating Toxin p55 Domain'''
'''Crystal Structure of the Helicobacter pylori Vacuolating Toxin p55 Domain'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Gangwer, K A.]]
[[Category: Gangwer, K A.]]
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[[Category: beta-helix]]
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[[Category: Beta-helix]]
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[[Category: toxin]]
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[[Category: Toxin]]
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[[Category: vaca]]
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[[Category: Vaca]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:44:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:53:37 2008''
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Revision as of 12:44, 4 May 2008

Template:STRUCTURE 2qv3

Crystal Structure of the Helicobacter pylori Vacuolating Toxin p55 Domain


Overview

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.

About this Structure

2QV3 is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 15:44:19 2008

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