8IGW

Hexameric Ring Complex of Engineered V1-ATPase bound to 4 ADPs: A3(De)3_(ADP)3cat,1non-cat, Hexameric Ring Complex of Engineered V1-ATPase bound to 5 ADPs: A3(De)3_(ADP)3cat,2non-cat

これはPDB形式変換不可エントリーです。

「7COS」から置き換えられました

8IGW の概要

• エントリーDOI: 10.2210/pdb8igw/pdb
• 関連するPDBエントリー: 7COQ 7COS 8IGU 8IGV
• 分子名称: V-type sodium ATPase catalytic subunit A, V-type sodium ATPase subunit B, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: computational design, rotary molecular motor, complex, motor protein
• 由来する生物種: Enterococcus hirae ATCC 9790; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 706524.15

構造登録者

Kosugi, T.,Tanabe, M.,Koga, N. (登録日: 2023-02-21, 公開日: 2023-07-12, 最終更新日: 2025-03-12)

主引用文献

Kosugi, T.,Iida, T.,Tanabe, M.,Iino, R.,Koga, N.
Design of allosteric sites into rotary motor V 1 -ATPase by restoring lost function of pseudo-active sites.
Nat.Chem., 15:1591-1598, 2023

PubMed Abstract: Allostery produces concerted functions of protein complexes by orchestrating the cooperative work between the constituent subunits. Here we describe an approach to create artificial allosteric sites in protein complexes. Certain protein complexes contain subunits with pseudo-active sites, which are believed to have lost functions during evolution. Our hypothesis is that allosteric sites in such protein complexes can be created by restoring the lost functions of pseudo-active sites. We used computational design to restore the lost ATP-binding ability of the pseudo-active site in the B subunit of a rotary molecular motor, V-ATPase. Single-molecule experiments with X-ray crystallography analyses revealed that binding of ATP to the designed allosteric site boosts this V's activity compared with the wild-type, and the rotation rate can be tuned by modulating ATP's binding affinity. Pseudo-active sites are widespread in nature, and our approach shows promise as a means of programming allosteric control over concerted functions of protein complexes.

PubMed: 37414880
DOI: 10.1038/s41557-023-01256-4

実験手法

X-RAY DIFFRACTION (4.2 Å)