3SKY

2.1A crystal structure of the phosphate bound ATP binding domain of Archaeoglobus fulgidus COPB

3SKY の概要

• エントリーDOI: 10.2210/pdb3sky/pdb
• 関連するPDBエントリー: 3SKX
• 分子名称: Copper-exporting P-type ATPase B, PHOSPHATE ION, 3[N-MORPHOLINO]PROPANE SULFONIC ACID, ... (4 entities in total)
• 機能のキーワード: p1b-atpase, atp binding domain, copper(ii) transporter, membrane protein, amppnp, phosphate ion, hydrolase
• 由来する生物種: Archaeoglobus fulgidus
• 細胞内の位置: Cell membrane; Multi-pass membrane protein (Potential): O30085
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30442.55

構造登録者

Jayakanthan, S.,Roberts, S.A.,Weichsel, A.,Arguello, J.M.,McEvoy, M.M. (登録日: 2011-06-23, 公開日: 2012-06-20, 最終更新日: 2024-02-28)

主引用文献

Jayakanthan, S.,Roberts, S.A.,Weichsel, A.,Arguello, J.M.,McEvoy, M.M.
Conformations of the apo-, substrate-bound and phosphate-bound ATP-binding domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to the catalytic cycle.
Biosci.Rep., 32:443-453, 2012

PubMed Abstract: Heavy metal P1B-type ATPases play a critical role in cell survival by maintaining appropriate intracellular metal concentrations. Archaeoglobus fulgidus CopB is a member of this family that transports Cu(II) from the cytoplasm to the exterior of the cell using ATP as energy source. CopB has a 264 amino acid ATPBD (ATP-binding domain) that is essential for ATP binding and hydrolysis as well as ultimately transducing the energy to the transmembrane metal-binding site for metal occlusion and export. The relevant conformations of this domain during the different steps of the catalytic cycle are still under discussion. Through crystal structures of the apo- and phosphate-bound ATPBDs, with limited proteolysis and fluorescence studies of the apo- and substrate-bound states, we show that the isolated ATPBD of CopB cycles from an open conformation in the apo-state to a closed conformation in the substrate-bound state, then returns to an open conformation suitable for product release. The present work is the first structural report of an ATPBD with its physiologically relevant product (phosphate) bound. The solution studies we have performed help resolve questions on the potential influence of crystal packing on domain conformation. These results explain how phosphate is co-ordinated in ATPase transporters and give an insight into the physiologically relevant conformation of the ATPBD at different steps of the catalytic cycle.

PubMed: 22663904
DOI: 10.1042/BSR20120048

実験手法

X-RAY DIFFRACTION (2.1 Å)