1oq3

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[[Image:1oq3.jpg|left|200px]]
 
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{{Structure
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==A core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilis==
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|PDB= 1oq3 |SIZE=350|CAPTION= <scene name='initialview01'>1oq3</scene>
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<StructureSection load='1oq3' size='340' side='right'caption='[[1oq3]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1oq3]] 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=1OQ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OQ3 FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Copper-exporting_ATPase Copper-exporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.4 3.6.3.4] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= YVGX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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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=1oq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oq3 OCA], [https://pdbe.org/1oq3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oq3 RCSB], [https://www.ebi.ac.uk/pdbsum/1oq3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oq3 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1opz|1OPZ]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oq3 OCA], [http://www.ebi.ac.uk/pdbsum/1oq3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oq3 RCSB]</span>
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[https://www.uniprot.org/uniprot/COPA_BACSU COPA_BACSU] Involved in copper export.<ref>PMID:12644235</ref>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''A core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilis'''
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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/oq/1oq3_consurf.spt"</scriptWhenChecked>
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==Overview==
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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=1oq3 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 ==
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.
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.
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==About this Structure==
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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>
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1OQ3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQ3 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12888353 12888353]
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</div>
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<div class="pdbe-citations 1oq3" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Copper-exporting ATPase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Banci L]]
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[[Category: Banci, L.]]
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[[Category: Bertini I]]
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[[Category: Bertini, I.]]
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[[Category: Ciofi-Baffoni S]]
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[[Category: Ciofi-Baffoni, S.]]
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[[Category: Gonnelli L]]
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[[Category: Gonnelli, L.]]
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[[Category: Su XC]]
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[[Category: SPINE, Structural Proteomics in Europe.]]
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[[Category: Su, X C.]]
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[[Category: copa;nmr;folding;p-type atpase;mutation]]
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[[Category: spine]]
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[[Category: structural genomic]]
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[[Category: structural proteomics in europe]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:48:43 2008''
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Current revision

A core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilis

PDB ID 1oq3

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