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Structure paper

TitleNucleotide recognition by CopA, a Cu+-transporting P-type ATPase.
Journal, issue, pagesEmbo J., Vol. 28, Page 1782-1791, Year 2009
Publish dateMar 31, 2009 (structure data deposition date)
AuthorsTsuda, T. / Toyoshima, C.
External linksEmbo J. / PubMed:19478797
MethodsX-ray diffraction
Resolution1.85 - 1.95 Å
Structure data

PDB-3a1c:
crystal structure of the P- and N-domains of CopA, a copper-transporting P-type ATPase, bound with AMPPCP-Mg
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-3a1d:
Crystal structure of the P- and N-domains of CopA, a copper-transporting P-type ATPase, bound with ADP-Mg
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-3a1e:
Crystal structure of the P- and N-domains of His462Gln mutant CopA, a copper-transporting P-type ATPase, bound with AMPPCP-Mg
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-ACP:
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / AMP-PCP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • archaeoglobus fulgidus (archaea)
KeywordsHYDROLASE / P-type ATPase / ATP-binding / Cell membrane / Copper transport / Ion transport / Magnesium / Membrane / Metal-binding / Nucleotide-binding / Phosphoprotein / Transmembrane / Transport

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