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1ouv

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{{Seed}}
 
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[[Image:1ouv.png|left|200px]]
 
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==Helicobacter cysteine rich protein C (HcpC)==
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The line below this paragraph, containing "STRUCTURE_1ouv", creates the "Structure Box" on the page.
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<StructureSection load='1ouv' size='340' side='right'caption='[[1ouv]], [[Resolution|resolution]] 2.00&Aring;' 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'>[[1ouv]] is a 1 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=1OUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OUV FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ouv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ouv OCA], [https://pdbe.org/1ouv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ouv RCSB], [https://www.ebi.ac.uk/pdbsum/1ouv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ouv ProSAT]</span></td></tr>
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{{STRUCTURE_1ouv| PDB=1ouv | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HCPC_HELPY HCPC_HELPY] May hydrolyze 6-aminopenicillinic acid and 7-aminocephalosporanic acid (ACA) derivatives (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ou/1ouv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ouv ConSurf].
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<div style="clear:both"></div>
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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 Gram-negative human pathogen that infects the gastric mucosa and causes an inflammatory process leading to gastritis, ulceration and cancer. Bacterial cell-surface and secreted proteins often play an important role in pathogen-host interactions and are thought to be selective mediators for the pathology of the infection. The Helicobacter cysteine-rich proteins (Hcp) represent a large family of secreted proteins that seem to be specific for microorganisms from the epsilon-subfamily of proteobacteria. Although significantly elevated levels of anti-Hcp antibodies were observed in many patients infected with H.pylori, details on the biological functions of Hcp proteins are sparse. Hcps belong to a large family of Sel1-like multi-repeat proteins. The crystal structure of HcpC was refined at 2.0 A resolution and revealed a super-helical topology composed of seven disulfide bridged alpha/alpha-repeats, an N-terminal capping helix and an extended C-terminal coil consisting of alternating hydrophobic and hydrophilic residues. In the crystal packing, the C-terminal coil interacts with the concave surface of a symmetry-related HcpC super-helix. A hydrophobic pocket and a cluster of negatively charged residues recognize the side-chains of Val290 and Lys287 from the C-terminal coil, respectively. The peptide nitrogen atom of His291 forms a short hydrogen bond with the side-chain of Asn66. The interactions seen in this crystal contact are strikingly similar to the peptide-binding modes of the Hsp70/Hsp90 organizing protein and the PEX5 receptor. The conservation of the peptide-binding mode suggests that HcpC might recognize its binding partner in a similar way.
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===Helicobacter cysteine rich protein C (HcpC)===
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The crystal structure of Helicobacter cysteine-rich protein C at 2.0 A resolution: similar peptide-binding sites in TPR and SEL1-like repeat proteins.,Luthy L, Grutter MG, Mittl PR J Mol Biol. 2004 Jul 16;340(4):829-41. PMID:15223324<ref>PMID:15223324</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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<!--
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_15223324}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1ouv" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15223324 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15223324}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Helicobacter pylori 26695]]
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1OUV is a [[Single protein]] structure of 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=1OUV OCA].
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[[Category: Large Structures]]
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[[Category: Luethy L]]
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==Reference==
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[[Category: Mittl PR]]
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The crystal structure of Helicobacter cysteine-rich protein C at 2.0 A resolution: similar peptide-binding sites in TPR and SEL1-like repeat proteins., Luthy L, Grutter MG, Mittl PR, J Mol Biol. 2004 Jul 16;340(4):829-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15223324 15223324]
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[[Category: Helicobacter pylori]]
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[[Category: Single protein]]
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[[Category: Luethy, L.]]
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[[Category: Mittl, P R.]]
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[[Category: Cysteine rich protein]]
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[[Category: Hcp repeat]]
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[[Category: Loop-helix-turn-helix]]
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[[Category: Repeat protein]]
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[[Category: Tpr repeat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:36:02 2008''
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Current revision

Helicobacter cysteine rich protein C (HcpC)

PDB ID 1ouv

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