3a1e: Difference between revisions
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<StructureSection load='3a1e' size='340' side='right'caption='[[3a1e]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='3a1e' size='340' side='right'caption='[[3a1e]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3a1e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3a1e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A1E FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3a1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a1e OCA], [https://pdbe.org/3a1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a1e RCSB], [https://www.ebi.ac.uk/pdbsum/3a1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a1e ProSAT]</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=3a1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a1e OCA], [https://pdbe.org/3a1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a1e RCSB], [https://www.ebi.ac.uk/pdbsum/3a1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a1e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/COPA_ARCFU COPA_ARCFU] Probably involved in copper and silver export.<ref>PMID:11756450</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Archaeoglobus fulgidus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Toyoshima | [[Category: Toyoshima C]] | ||
[[Category: Tsuda | [[Category: Tsuda T]] | ||
Latest revision as of 17:06, 1 November 2023
Crystal structure of the P- and N-domains of His462Gln mutant CopA, a copper-transporting P-type ATPase, bound with AMPPCP-MgCrystal structure of the P- and N-domains of His462Gln mutant CopA, a copper-transporting P-type ATPase, bound with AMPPCP-Mg
Structural highlights
FunctionCOPA_ARCFU Probably involved in copper and silver export.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHeavy metal pumps constitute a large subgroup in P-type ion-transporting ATPases. One of the outstanding features is that the nucleotide binding N-domain lacks residues critical for ATP binding in other well-studied P-type ATPases. Instead, they possess an HP-motif and a Gly-rich sequence in the N-domain, and their mutations impair ATP binding. Here, we describe 1.85 A resolution crystal structures of the P- and N-domains of CopA, an archaeal Cu(+)-transporting ATPase, with bound nucleotides. These crystal structures show that CopA recognises the adenine ring completely differently from other P-type ATPases. The crystal structure of the His462Gln mutant, in the HP-motif, a disease-causing mutation in human Cu(+)-ATPases, shows that the Gln side chain mimics the imidazole ring, but only partially, explaining the reduction in ATPase activity. These crystal structures lead us to propose a role of the His and a mechanism for removing Mg(2+) from ATP before phosphoryl transfer. Nucleotide recognition by CopA, a Cu+-transporting P-type ATPase.,Tsuda T, Toyoshima C EMBO J. 2009 Jun 17;28(12):1782-91. Epub 2009 May 28. PMID:19478797[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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