3J08

High resolution helical reconstruction of the bacterial p-type ATPase copper transporter CopA

3J08 の概要

• エントリーDOI: 10.2210/pdb3j08/pdb
• EMDBエントリー: 5271
• 分子名称: copper-exporting P-type ATPase A (1 entity in total)
• 機能のキーワード: p-type atpase, copper transporter, copa, adenosine triphosphatases, archaeal proteins, cation transport proteins, cryoelectron microscopy, hydrolase, metal transport
• 由来する生物種: Archaeoglobus fulgidus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 138427.58

構造登録者

Wu, C.,Allen, G.S.,Cardozo, T.,Stokes, D.L. (登録日: 2011-05-09, 公開日: 2011-08-24, 最終更新日: 2024-02-21)

主引用文献

Allen, G.S.,Wu, C.C.,Cardozo, T.,Stokes, D.L.
The Architecture of CopA from Archeaoglobus fulgidus Studied by Cryo-Electron Microscopy and Computational Docking.
Structure, 19:1219-1232, 2011

PubMed Abstract: CopA uses ATP to pump Cu(+) across cell membranes. X-ray crystallography has defined atomic structures of several related P-type ATPases. We have determined a structure of CopA at 10 Å resolution by cryo-electron microscopy of a new crystal form and used computational molecular docking to study the interactions between the N-terminal metal-binding domain (NMBD) and other elements of the molecule. We found that the shorter-chain lipids used to produce these crystals are associated with movements of the cytoplasmic domains, with a novel dimer interface and with disordering of the NMBD, thus offering evidence for the transience of its interaction with the other cytoplasmic domains. Docking identified a binding site that matched the location of the NMBD in our previous structure by cryo-electron microscopy, allowing a more detailed view of its binding configuration and further support for its role in autoinhibition.

PubMed: 21820315
DOI: 10.1016/j.str.2011.05.014

実験手法

ELECTRON MICROSCOPY (10 Å)