3A1C

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

3A1C の概要

• エントリーDOI: 10.2210/pdb3a1c/pdb
• 関連するPDBエントリー: 2ARF 2B8E 2IYE 3A1D 3A1E
• 分子名称: Probable copper-exporting P-type ATPase A, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: p-type atpase, atp-binding, cell membrane, copper transport, hydrolase, ion transport, magnesium, membrane, metal-binding, nucleotide-binding, phosphoprotein, transmembrane, transport
• 由来する生物種: Archaeoglobus fulgidus
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: O29777
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62597.49

構造登録者

Tsuda, T.,Toyoshima, C. (登録日: 2009-03-31, 公開日: 2009-07-21, 最終更新日: 2023-11-01)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.85 Å)