3VR5

Crystal structure of nucleotide-free Enterococcus hirae V1-ATPase [eV1(L)]

3VR5 の概要

• エントリーDOI: 10.2210/pdb3vr5/pdb
• 関連するPDBエントリー: 3VR2 3VR3 3VR4 3VR6
• 分子名称: V-type sodium ATPase catalytic subunit A, V-type sodium ATPase subunit B, V-type sodium ATPase subunit D, ... (4 entities in total)
• 機能のキーワード: v-atpase, enterococcus hirae, rotary motor, p-loop, hydrolase, na(+)-atpase, atp binding
• 由来する生物種: Enterococcus hirae; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 398063.88

構造登録者

Saijo, S.,Arai, S.,Suzuki, K.,Mizutani, K.,Kakinuma, Y.,Ishizuka-Katsura, Y.,Ohsawa, N.,Terada, T.,Shirouzu, M.,Yokoyama, S.,Iwata, S.,Yamato, I.,Murata, T. (登録日: 2012-04-03, 公開日: 2013-01-16, 最終更新日: 2024-10-16)

主引用文献

Arai, S.,Saijo, S.,Suzuki, K.,Mizutani, K.,Kakinuma, Y.,Ishizuka-Katsura, Y.,Ohsawa, N.,Terada, T.,Shirouzu, M.,Yokoyama, S.,Iwata, S.,Yamato, I.,Murata, T.
Rotation mechanism of Enterococcus hirae V(1)-ATPase based on asymmetric crystal structures
Nature, 493:703-707, 2013

PubMed Abstract: In various cellular membrane systems, vacuolar ATPases (V-ATPases) function as proton pumps, which are involved in many processes such as bone resorption and cancer metastasis, and these membrane proteins represent attractive drug targets for osteoporosis and cancer. The hydrophilic V(1) portion is known as a rotary motor, in which a central axis DF complex rotates inside a hexagonally arranged catalytic A(3)B(3) complex using ATP hydrolysis energy, but the molecular mechanism is not well defined owing to a lack of high-resolution structural information. We previously reported on the in vitro expression, purification and reconstitution of Enterococcus hirae V(1)-ATPase from the A(3)B(3) and DF complexes. Here we report the asymmetric structures of the nucleotide-free (2.8 Å) and nucleotide-bound (3.4 Å) A(3)B(3) complex that demonstrate conformational changes induced by nucleotide binding, suggesting a binding order in the right-handed rotational orientation in a cooperative manner. The crystal structures of the nucleotide-free (2.2 Å) and nucleotide-bound (2.7 Å) V(1)-ATPase are also reported. The more tightly packed nucleotide-binding site seems to be induced by DF binding, and ATP hydrolysis seems to be stimulated by the approach of a conserved arginine residue. To our knowledge, these asymmetric structures represent the first high-resolution view of the rotational mechanism of V(1)-ATPase.

PubMed: 23334411
DOI: 10.1038/nature11778

実験手法

X-RAY DIFFRACTION (3.9 Å)