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TitleSolution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states.
Journal, issue, pagesJ. Mol. Biol., Vol. 317, Page 415-429, Year 2002
Publish dateSep 5, 2001 (structure data deposition date)
AuthorsBanci, L. / Bertini, I. / Ciofi-Baffoni, S. / D'Onofrio, M. / Gonnelli, L. / Marhuenda-Egea, F.C. / Ruiz-Duenas, F.J.
External linksJ. Mol. Biol. / PubMed:11922674
MethodsNMR (solution)
Structure data

PDB-1jww:
NMR characterization of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis
Method: SOLUTION NMR

PDB-1kqk:
Solution Structure of the N-terminal Domain of a Potential Copper-translocating P-type ATPase from Bacillus subtilis in the Cu(I)loaded State
Method: SOLUTION NMR

Chemicals

ChemComp-CU1:
COPPER (I) ION

Source
  • bacillus subtilis (bacteria)
KeywordsHYDROLASE / beta-alpha-beta-beta-alpha-beta / CopA / folding / P-type ATPase / copper transporting protein

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