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TitleThe architecture of CopA from Archeaoglobus fulgidus studied by cryo-electron microscopy and computational docking.
Journal, issue, pagesStructure, Vol. 19, Issue 9, Page 1219-1232, Year 2011
Publish dateSep 7, 2011
AuthorsGregory S Allen / Chen-Chou Wu / Tim Cardozo / David L Stokes /
PubMed AbstractCopA 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 Å resolution ...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 Å 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.
External linksStructure / PubMed:21820315 / PubMed Central
MethodsEM (helical sym.)
Resolution10.0 Å
Structure data

5271

3j08

EMDB-5271: High resolution helical reconstruction of the bacterial p-type ATPase copper transporter CopA.
PDB-3j08: High resolution helical reconstruction of the bacterial p-type ATPase copper transporter CopA
Method: EM (helical sym.) / Resolution: 10.0 Å

PDB-3j09:
High resolution helical reconstruction of the bacterial p-type ATPase copper transporter CopA
Method: ELECTRON MICROSCOPY / Resolution: 10 Å

Source
  • archaeoglobus fulgidus (archaea)
KeywordsHYDROLASE / METAL TRANSPORT / p-type ATPase / copper transporter / CopA / adenosine triphosphatases / archaeal proteins / cation transport proteins / cryoelectron microscopy

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