1oq6: Difference between revisions

← Older edit

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

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1oq6.png|left|200px]]
-<!--
+==solution structure of Copper-S46V CopA from Bacillus subtilis==
-The line below this paragraph, containing "STRUCTURE_1oq6", creates the "Structure Box" on the page.
+<StructureSection load='1oq6' size='340' side='right'caption='[[1oq6]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1oq6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OQ6 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
-{{STRUCTURE_1oq6|  PDB=1oq6  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oq6 OCA], [https://pdbe.org/1oq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oq6 RCSB], [https://www.ebi.ac.uk/pdbsum/1oq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oq6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/COPA_BACSU COPA_BACSU] Involved in copper export.<ref>PMID:12644235</ref>
+== 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/oq/1oq6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1oq6 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The two N-terminal domains of the P-type copper ATPase, CopAa and CopAb, from Bacillus subtilis differ in their folding capabilities in vitro. Whereas CopAb has the typical betaalphabetabetaalphabeta structure and is a rigid protein, CopAa is found to be largely unfolded. A sequence analysis of the two and of orthologue homologous proteins indicates that Ser46 in CopAa may destabilise the hydrophobic core, as also confirmed through a bioinformatic energy study. CopAb has a Val in the corresponding position. The S46V and S46A mutants are found to be folded, although the latter displays multiple conformations. S46VCopAa, in both apo and copper(I) loaded forms, has very similar structural and dynamic properties with respect to CopAb, besides a different length of strand beta2 and beta4. It is intriguing that the oxygen of Thr16 is found close, though at longer than bonding distance, to copper in both domains, as it also occurs in a human orthologue domain. This study contributes to understanding the behaviour of proteins that do not properly fold in vitro. A possible biological significance of the peculiar folding behaviour of this domain is discussed.
-===solution structure of Copper-S46V CopA from Bacillus subtilis===
+A core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilis.,Banci L, Bertini I, Ciofi-Baffoni S, Gonnelli L, Su XC J Mol Biol. 2003 Aug 8;331(2):473-84. PMID:12888353<ref>PMID:12888353</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_12888353}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1oq6" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 12888353 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_12888353}}
+__TOC__
+</StructureSection>
-==About this Structure==
-OQ6 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQ6 OCA].
-==Reference==
-<ref group="xtra">PMID:12888353</ref><references group="xtra"/>
 [[Category: Bacillus subtilis]]
-[[Category: Copper-exporting ATPase]]
+[[Category: Large Structures]]
-[[Category: Banci, L.]]
+[[Category: Banci L]]
-[[Category: Bertini, I.]]
+[[Category: Bertini I]]
-[[Category: Ciofi-Baffoni, S.]]
+[[Category: Ciofi-Baffoni S]]
-[[Category: Gonnelli, l.]]
+[[Category: Gonnelli l]]
-[[Category: SPINE, Structural Proteomics in Europe.]]
+[[Category: Su XC]]
-[[Category: Su, X C.]]
-[[Category: Copper complex]]
-[[Category: Folding]]
-[[Category: Mutation]]
-[[Category: Nmr]]
-[[Category: P-type atpase]]
-[[Category: Spine]]
-[[Category: Structural genomic]]
-[[Category: Structural proteomics in europe]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 04:21:31 2009''