3j08: Difference between revisions

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== Function ==
== Function ==
[https://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>  
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== Publication Abstract from PubMed ==
CopA uses ATP to pump Cu(+) across cell membranes. X-ray crystallography has defined atomic structures of several related P-type ATPases. We have determined a structure of CopA at 10 A resolution by cryo-electron microscopy of a new crystal form and used computational molecular docking to study the interactions between the N-terminal metal-binding domain (NMBD) and other elements of the molecule. We found that the shorter-chain lipids used to produce these crystals are associated with movements of the cytoplasmic domains, with a novel dimer interface and with disordering of the NMBD, thus offering evidence for the transience of its interaction with the other cytoplasmic domains. Docking identified a binding site that matched the location of the NMBD in our previous structure by cryo-electron microscopy, allowing a more detailed view of its binding configuration and further support for its role in autoinhibition.
The Architecture of CopA from Archeaoglobus fulgidus Studied by Cryo-Electron Microscopy and Computational Docking.,Allen GS, Wu CC, Cardozo T, Stokes DL Structure. 2011 Aug 3. PMID:21820315<ref>PMID:21820315</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
==See Also==

Latest revision as of 13:08, 21 February 2024

High resolution helical reconstruction of the bacterial p-type ATPase copper transporter CopAHigh resolution helical reconstruction of the bacterial p-type ATPase copper transporter CopA

3j08, resolution 10.00Å

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OCA