3EIU

A second transient position of ATP on its trail to the nucleotide-binding site of subunit B of the motor protein A1Ao ATP synthase

3EIU の概要

• エントリーDOI: 10.2210/pdb3eiu/pdb
• 関連するPDBエントリー: 2C61 2RKW 3B2Q 3DSR
• 分子名称: V-type ATP synthase beta chain, ADENOSINE-5'-TRIPHOSPHATE, 4-(2-AMINOETHYL)BENZENESULFONYL FLUORIDE (3 entities in total)
• 機能のキーワード: hydrolase, atp synthesis, hydrogen ion transport, ion transport, transport
• 由来する生物種: Methanosarcina mazei (Methanosarcina frisia)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 103877.79

構造登録者

Manimekalai, S.M.S.,Kumar, A.,Balakrishna, A.M.,Gruber, G. (登録日: 2008-09-17, 公開日: 2009-02-10, 最終更新日: 2023-11-01)

主引用文献

Manimekalai, M.S.S.,Kumar, A.,Balakrishna, A.M.,Gruber, G.
A second transient position of ATP on its trail to the nucleotide-binding site of subunit B of the motor protein A(1)A(O) ATP synthase
J.Struct.Biol., 166:38-45, 2009

PubMed Abstract: The adenosine triphosphate (ATP) entrance into the nucleotide-binding subunits of ATP synthases is a puzzle. In the previously determined structure of subunit B mutant R416W of the Methanosarcina mazei Gö1 A-ATP synthase one ATP could be trapped at a transition position, close to the phosphate-binding loop. Using defined parameters for co-crystallization of an ATP-bound B-subunit, a unique transition position of ATP could be found in the crystallographic structure of this complex, solved at 3.4 A resolution. The nucleotide is found near the helix-turn-helix motif in the C-terminal domain of the protein; the location occupied by the gamma-subunit to interact with the empty beta-subunit in the thermoalkaliphilic Bacillus sp. TA2.A1 of the related F-ATP synthase. When compared with the determined structure of the ATP-transition position, close to the P-loop, and the nucleotide-free form of subunit B, the C-terminal domain of the B mutant is rotated by around 6 degrees, implicating an ATP moving pathway. We propose that, in the nucleotide empty state the central stalk subunit D is in close contact with subunit B and when the ATP molecule enters, D moves slightly, paving way for it to interact with the subunit B, which makes the C-terminal domain rotate by 6 degrees.

PubMed: 19138746
DOI: 10.1016/j.jsb.2008.12.004

実験手法

X-RAY DIFFRACTION (3.43 Å)