3P20

Crystal structure of vanadate bound subunit A of the A1AO ATP synthase

3P20 の概要

• エントリーDOI: 10.2210/pdb3p20/pdb
• 関連するPDBエントリー: 3I4L 3I72 3I73 3IKJ 3M4Y 3MFY
• 分子名称: V-type ATP synthase alpha chain, VANADATE ION, ACETIC ACID, ... (6 entities in total)
• 機能のキーワード: hydrolase, atp binding
• 由来する生物種: Pyrococcus horikoshii; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 66842.66

構造登録者

Manimekalai, M.S.S.,Kumar, A.,Jeyakanthan, J.,Gruber, G. (登録日: 2010-10-01, 公開日: 2011-03-30, 最終更新日: 2023-11-01)

主引用文献

Manimekalai, M.S.,Kumar, A.,Jeyakanthan, J.,Gruber, G.
The transition-like state and Pi entrance into the catalytic a subunit of the biological engine A-ATP synthase.
J.Mol.Biol., 408:736-754, 2011

PubMed Abstract: Archaeal A-ATP synthases catalyze the formation of the energy currency ATP. The chemical mechanisms of ATP synthesis in A-ATP synthases are unknown. We have determined the crystal structure of a transition-like state of the vanadate-bound form of catalytic subunit A (A(Vi)) of the A-ATP synthase from Pyrococcus horikoshii OT3. Two orthovanadate molecules were observed in the A(Vi) structure, one of which interacts with the phosphate binding loop through residue S238. The second vanadate is positioned in the transient binding site, implicating for the first time the pathway for phosphate entry to the catalytic site. Moreover, since residues K240 and T241 are proposed to be essential for catalysis, the mutant structures of K240A and T241A were also determined. The results demonstrate the importance of these two residues for transition-state stabilization. The structures presented shed light on the diversity of catalytic mechanisms used by the biological motors A- and F-ATP synthases and eukaryotic V-ATPases.

PubMed: 21396943
DOI: 10.1016/j.jmb.2011.03.010

実験手法

X-RAY DIFFRACTION (2.85 Å)