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==Crystal structure of the P- and N-domains of His462Gln mutant CopA, a copper-transporting P-type ATPase, bound with AMPPCP-Mg==
==Crystal structure of the P- and N-domains of His462Gln mutant CopA, a copper-transporting P-type ATPase, bound with AMPPCP-Mg==
<StructureSection load='3a1e' size='340' side='right' caption='[[3a1e]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='3a1e' size='340' side='right'caption='[[3a1e]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3a1e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A1E FirstGlance]. <br>
<table><tr><td colspan='2'>[[3a1e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arcfl Arcfl]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a1c|3a1c]], [[3a1d|3a1d]], [[2b8e|2b8e]], [[2iye|2iye]], [[2arf|2arf]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3a1c|3a1c]], [[3a1d|3a1d]], [[2b8e|2b8e]], [[2iye|2iye]], [[2arf|2arf]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">copA, pacS, AF_0473 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 ARCFL])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">copA, pacS, AF_0473 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 ARCFL])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3a1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a1e OCA], [http://pdbe.org/3a1e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a1e RCSB], [http://www.ebi.ac.uk/pdbsum/3a1e PDBsum], [http://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 ==
[[http://www.uniprot.org/uniprot/COPA_ARCFU COPA_ARCFU]] Probably involved in copper and silver export.<ref>PMID:11756450</ref>   
[[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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==See Also==
==See Also==
*[[ATPase|ATPase]]
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Arcfl]]
[[Category: Arcfl]]
[[Category: Large Structures]]
[[Category: Toyoshima, C]]
[[Category: Toyoshima, C]]
[[Category: Tsuda, T]]
[[Category: Tsuda, T]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: P-type atpase]]
[[Category: P-type atpase]]

Revision as of 10:21, 10 November 2021

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

3a1e is a 2 chain structure with sequence from Arcfl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:copA, pacS, AF_0473 (ARCFL)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[COPA_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 PubMed

Heavy 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 Also

References

  1. Mandal AK, Cheung WD, Arguello JM. Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the extremophile Archaeoglobus fulgidus. J Biol Chem. 2002 Mar 1;277(9):7201-8. Epub 2001 Dec 26. PMID:11756450 doi:10.1074/jbc.M109964200
  2. Tsuda T, Toyoshima C. Nucleotide recognition by CopA, a Cu+-transporting P-type ATPase. EMBO J. 2009 Jun 17;28(12):1782-91. Epub 2009 May 28. PMID:19478797 doi:10.1038/emboj.2009.143

3a1e, resolution 1.95Å

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