3A1D

Crystal structure of the P- and N-domains of CopA, a copper-transporting P-type ATPase, bound with ADP-Mg

Summary for 3A1D

• Entry DOI: 10.2210/pdb3a1d/pdb
• Related: 2ARF 2B8E 2IYE 3A1C 3A1E
• Descriptor: Probable copper-exporting P-type ATPase A, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: p-type atpase, hydrolase
• Biological source: Archaeoglobus fulgidus
• Cellular location: Cell membrane; Multi-pass membrane protein: O29777
• Total number of polymer chains: 2
• Total formula weight: 62465.78

Authors

Tsuda, T.,Toyoshima, C. (deposition date: 2009-03-31, release date: 2009-07-21, Last modification date: 2023-11-01)

Primary citation

Tsuda, T.,Toyoshima, C.
Nucleotide recognition by CopA, a Cu+-transporting P-type ATPase.
Embo J., 28:1782-1791, 2009

PubMed Abstract: 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.

PubMed: 19478797
DOI: 10.1038/emboj.2009.143

Experimental method

X-RAY DIFFRACTION (1.85 Å)