1sew

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:1sew.png|left|200px]]
 
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==MEMBRANE CHANNEL STRUCTURE OF HELICOBACTER PYLORI VACUOLATING TOXIN A==
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The line below this paragraph, containing "STRUCTURE_1sew", creates the "Structure Box" on the page.
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<StructureSection load='1sew' size='340' side='right'caption='[[1sew]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SEW FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sew FirstGlance], [https://www.ebi.ac.uk/pdbsum/1sew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sew ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1sew| PDB=1sew | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===MEMBRANE CHANNEL STRUCTURE OF HELICOBACTER PYLORI VACUOLATING TOXIN A===
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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<ref>PMID:15067113</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_15067113}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1sew" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15067113 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15067113}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SEW OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:15067113</ref><references group="xtra"/>
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[[Category: Bowie, J U]]
[[Category: Bowie, J U]]
[[Category: Chamberlain, A K]]
[[Category: Chamberlain, A K]]
[[Category: Kim, S]]
[[Category: Kim, S]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 07:53:54 2010''
 

Current revision

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

PDB ID 1sew

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