1opz: Difference between revisions

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 ==A core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilis==
-<StructureSection load='1opz' size='340' side='right'caption='[[1opz]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+<StructureSection load='1opz' size='340' side='right'caption='[[1opz]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1opz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OPZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OPZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1opz]] 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=1OPZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OPZ FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1oq3|1oq3]], [[1oq6|1oq6]]</div></td></tr>
+</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YVGX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Copper-exporting_ATPase Copper-exporting ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.4 3.6.3.4] </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=1opz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1opz OCA], [https://pdbe.org/1opz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1opz RCSB], [https://www.ebi.ac.uk/pdbsum/1opz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1opz ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/COPA_BACSU COPA_BACSU]] Involved in copper export.<ref>PMID:12644235</ref>
+[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]]
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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=1opz 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.
-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>
-<div class="pdbe-citations 1opz" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Vibrio subtilis ehrenberg 1835]]
+[[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: Gonneli, L]]
+[[Category: Gonneli L]]
-[[Category: Su, X C]]
+[[Category: Su XC]]
-[[Category: Abbab fold]]
-[[Category: Folding]]
-[[Category: Hydrolase]]
-[[Category: Mutation]]