3A5D

Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase

3A5D の概要

• エントリーDOI: 10.2210/pdb3a5d/pdb
• 関連するPDBエントリー: 3A5C
• 分子名称: V-type ATP synthase alpha chain, V-type ATP synthase beta chain, V-type ATP synthase subunit D, ... (4 entities in total)
• 機能のキーワード: v-atpase, asymmetric, rotation, vacuolar type, hydrolase, atp synthesis, atp-binding, hydrogen ion transport, ion transport, nucleotide-binding, transport
• 由来する生物種: Thermus thermophilus; 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 773537.82

構造登録者

Numoto, N.,Hasegawa, Y.,Takeda, K.,Miki, K. (登録日: 2009-08-06, 公開日: 2009-10-13, 最終更新日: 2023-11-01)

主引用文献

Numoto, N.,Hasegawa, Y.,Takeda, K.,Miki, K.
Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase
Embo Rep., 10:1228-1234, 2009

PubMed Abstract: V-type ATPases (V-ATPases) are categorized as rotary ATP synthase/ATPase complexes. The V-ATPases are distinct from F-ATPases in terms of their rotation scheme, architecture and subunit composition. However, there is no detailed structural information on V-ATPases despite the abundant biochemical and biophysical research. Here, we report a crystallographic study of V1-ATPase, from Thermus thermophilus, which is a soluble component consisting of A, B, D and F subunits. The structure at 4.5 A resolution reveals inter-subunit interactions and nucleotide binding. In particular, the structure of the central stalk composed of D and F subunits was shown to be characteristic of V1-ATPases. Small conformational changes of respective subunits and significant rearrangement of the quaternary structure observed in the three AB pairs were related to the interaction with the straight central stalk. The rotation mechanism is discussed based on a structural comparison between V1-ATPases and F1-ATPases.

PubMed: 19779483
DOI: 10.1038/embor.2009.202

実験手法

X-RAY DIFFRACTION (4.8 Å)