1P6T

Structure characterization of the water soluble region of P-type ATPase CopA from Bacillus subtilis

1P6T の概要

• エントリーDOI: 10.2210/pdb1p6t/pdb
• 関連するPDBエントリー: 1KQK 1OQ3
• NMR情報: BMRB: 5813
• 分子名称: Potential copper-transporting ATPase (1 entity in total)
• 機能のキーワード: copa; p-type atpase; water-soluble region; beta-alpha-beta-beta-alpha-beta fold; nmr, structural proteomics in europe, spine, structural genomics, hydrolase
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: O32220
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16400.75

構造登録者

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Gonnelli, L.,Su, X.C.,Structural Proteomics in Europe (SPINE) (登録日: 2003-04-30, 公開日: 2003-12-16, 最終更新日: 2024-05-22)

主引用文献

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Gonnelli, L.,Su, X.C.
Structural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilis.
J.Biol.Chem., 278:50506-50513, 2003

PubMed Abstract: The solution structure of the N-terminal region (151 amino acids) of a copper ATPase, CopA, from Bacillus subtilis, is reported here. It consists of two domains, CopAa and CopAb, linked by two amino acids. It is found that the two domains, which had already been separately characterized, interact one to the other through a hydrogen bond network and a few hydrophobic interactions, forming a single rigid body. The two metal binding sites are far from one another, and the short link between the domains prevents them from interacting. This and the surface electrostatic potential suggest that each domain receives copper from the copper chaperone, CopZ, independently and transfers it to the membrane binding site of CopA. The affinity constants of silver(I) and copper(I) are similar for the two sites as monitored by NMR. Because the present construct "domain-short link-domain" is shared also by the last two domains of the eukaryotic copper ATPases and several residues at the interface between the two domains are conserved, the conclusions of the present study have general validity for the understanding of the function of copper ATPases.

PubMed: 14514665
DOI: 10.1074/jbc.M307389200

実験手法

SOLUTION NMR