1ouv: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ouv.gif|left|200px]]<br /><applet load="1ouv" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1ouv, resolution 2.&Aring;" />
-'''Helicobacter cysteine rich protein C (HcpC)'''<br />
-==Overview==
+==Helicobacter cysteine rich protein C (HcpC)==
-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.
+<StructureSection load='1ouv' size='340' side='right'caption='[[1ouv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HCPC_HELPY HCPC_HELPY] May hydrolyze 6-aminopenicillinic acid and 7-aminocephalosporanic acid (ACA) derivatives (By similarity).
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ou/1ouv_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==About this Structure==
+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>
-OUV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OUV OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15223324 15223324]
+</div>
-[[Category: Helicobacter pylori]]
+<div class="pdbe-citations 1ouv" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
+== References ==
-[[Category: Luethy, L.]]
+<references/>
-[[Category: Mittl, P.R.]]
+__TOC__
-[[Category: cysteine rich protein]]
+</StructureSection>
-[[Category: hcp repeat]]
+[[Category: Helicobacter pylori 26695]]
-[[Category: loop-helix-turn-helix]]
+[[Category: Large Structures]]
-[[Category: repeat protein]]
+[[Category: Luethy L]]
-[[Category: tpr repeat]]
+[[Category: Mittl PR]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:13:02 2007''