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3vnc

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Current revision (08:40, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3vnc' size='340' side='right'caption='[[3vnc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3vnc' size='340' side='right'caption='[[3vnc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vnc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VNC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vnc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VNC FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP_0596 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=3vnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vnc OCA], [https://pdbe.org/3vnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vnc RCSB], [https://www.ebi.ac.uk/pdbsum/3vnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vnc ProSAT]</span></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=3vnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vnc OCA], [https://pdbe.org/3vnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vnc RCSB], [https://www.ebi.ac.uk/pdbsum/3vnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vnc ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/O25318_HELPY O25318_HELPY]
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Tipalpha (TNF-alpha-inducing protein) from Helicobacter pylori is a carcinogenic effector. Studies on this protein revealed that a homodimer linked by a pair of intermolecular disulfide bridges (Cys25-Cys25 and Cys27-Cys27) was absolutely necessary for its biological functions. The activities of Tipalpha would be abolished when both disulfide bridges were disrupted. The crystal structures of Tipalpha reported to date, however, were based on inactive, monomeric mutants with their N-terminal, including residues Cys25 and Cys27, truncated. Here we report the crystal structure of H. pylori Tipalpha protein, TipalphaN(25), at 2.2A resolution, in which Cys25 and Cys27 form a pair of inter-chain disulfide bridges linking an active dimer. The disulfide bridges exhibit structural flexibility in the present structure. A series of structure-based mutagenesis, biochemical assays and molecular dynamic simulations on DNA-Tipalpha interactions reveal that Tipalpha utilizes the dimeric interface as the DNA-binding site and that residues His60, Arg77 and Arg81 located at the interface are crucial for DNA binding. Tipalpha could bind to one ssDNA, two ssDNA or one dsDNA in experiments, respectively, in the native or mutant states. The unique DNA-binding activities of Tipalpha indicate that the intrinsic flexible nature of disulfide bridges could endow certain elasticity to the Tipalpha dimer for its unique bioactivities. The results shed light on the possible structural mechanism for the functional performances of Tipalpha.
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Crystal Structure of TNF-alpha-Inducing Protein from Helicobacter Pylori in Active Form Reveals the Intrinsic Molecular Flexibility for Unique DNA-Binding.,Gao M, Li D, Hu Y, Zhang Y, Zou Q, Wang DC PLoS One. 2012;7(7):e41871. Epub 2012 Jul 31. PMID:22860022<ref>PMID:22860022</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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<div class="pdbe-citations 3vnc" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Campylobacter pylori]]
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[[Category: Helicobacter pylori 26695]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gao, M]]
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[[Category: Gao M]]
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[[Category: Hu, Y]]
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[[Category: Hu Y]]
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[[Category: Li, D]]
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[[Category: Li D]]
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[[Category: Wang, D C]]
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[[Category: Wang D-C]]
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[[Category: Zou, Q]]
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[[Category: Zou Q]]
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[[Category: Carcinogenic factor]]
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[[Category: Dna binding protein]]
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[[Category: Homodimer]]
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[[Category: Hp0596]]
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[[Category: Tnf-alpha-inducing protein]]
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Current revision

Crystal Structure of TIP-alpha N25 from Helicobacter Pylori in its natural dimeric form

PDB ID 3vnc

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