3guq: Difference between revisions
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[[ | ==Crystal structure of novel carcinogenic factor of H. pylori== | ||
<StructureSection load='3guq' size='340' side='right' caption='[[3guq]], [[Resolution|resolution]] 2.47Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3guq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GUQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GUQ FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP0596, HP_0596 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3guq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3guq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3guq RCSB], [http://www.ebi.ac.uk/pdbsum/3guq PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Stomach cancer is strongly associated with infection by Helicobacter pylori. In 2005, we identified a new H. pylori gene encoding a TNF-alpha inducing protein (Tipalpha) that acts as a carcinogenic factor. Tipalpha is secreted from H. pylori as a homodimer whose subunits are linked by disulfide bonds. We also characterized a Tipalpha deletion mutant (del-Tipalpha) that lacks the N-terminal six amino acid residues (LQACTC), including two cysteines (C5 and C7) that form disulfide bonds, but nonetheless shows a weak ability to induce TNF-alpha expression. Here we report that del-Tipalpha has a novel elongated structure containing a 40-A-long alpha helix, and forms a heart-shaped homodimer via non-covalent bonds. Moreover, their circular dichroism spectra strongly suggest that the structures of the del-Tipalpha and Tipalpha homodimers are very similar. del-Tipalpha's unique mode of dimer formation provides important insight into protein-protein interactions and into the mechanism underlying the carcinogenicity of H. pylori infection. | |||
Structural basis for the Helicobacter pylori-carcinogenic TNF-alpha-inducing protein.,Tsuge H, Tsurumura T, Utsunomiya H, Kise D, Kuzuhara T, Watanabe T, Fujiki H, Suganuma M Biochem Biophys Res Commun. 2009 Oct 16;388(2):193-8. Epub 2009 Jul 28. PMID:19643085<ref>PMID:19643085</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
[[Category: Fujiki, H | [[Category: Fujiki, H]] | ||
[[Category: Kise, D | [[Category: Kise, D]] | ||
[[Category: Kuzuhara, T | [[Category: Kuzuhara, T]] | ||
[[Category: Suganuma, M | [[Category: Suganuma, M]] | ||
[[Category: Tsuge, H | [[Category: Tsuge, H]] | ||
[[Category: Tsurumura, T | [[Category: Tsurumura, T]] | ||
[[Category: Utsunomiya, H | [[Category: Utsunomiya, H]] | ||
[[Category: Long alpha helix]] | [[Category: Long alpha helix]] | ||
[[Category: Novel carcinogenic factor]] | [[Category: Novel carcinogenic factor]] | ||
[[Category: Tnfa inducing factor]] | [[Category: Tnfa inducing factor]] | ||
[[Category: Toxin]] | [[Category: Toxin]] | ||
Revision as of 12:13, 8 December 2014
Crystal structure of novel carcinogenic factor of H. pyloriCrystal structure of novel carcinogenic factor of H. pylori
Structural highlights
Publication Abstract from PubMedStomach cancer is strongly associated with infection by Helicobacter pylori. In 2005, we identified a new H. pylori gene encoding a TNF-alpha inducing protein (Tipalpha) that acts as a carcinogenic factor. Tipalpha is secreted from H. pylori as a homodimer whose subunits are linked by disulfide bonds. We also characterized a Tipalpha deletion mutant (del-Tipalpha) that lacks the N-terminal six amino acid residues (LQACTC), including two cysteines (C5 and C7) that form disulfide bonds, but nonetheless shows a weak ability to induce TNF-alpha expression. Here we report that del-Tipalpha has a novel elongated structure containing a 40-A-long alpha helix, and forms a heart-shaped homodimer via non-covalent bonds. Moreover, their circular dichroism spectra strongly suggest that the structures of the del-Tipalpha and Tipalpha homodimers are very similar. del-Tipalpha's unique mode of dimer formation provides important insight into protein-protein interactions and into the mechanism underlying the carcinogenicity of H. pylori infection. Structural basis for the Helicobacter pylori-carcinogenic TNF-alpha-inducing protein.,Tsuge H, Tsurumura T, Utsunomiya H, Kise D, Kuzuhara T, Watanabe T, Fujiki H, Suganuma M Biochem Biophys Res Commun. 2009 Oct 16;388(2):193-8. Epub 2009 Jul 28. PMID:19643085[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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