1U7L

Crystal Structure of subunit C (vma5p) of the yeast V-ATPase

1U7L の概要

• エントリーDOI: 10.2210/pdb1u7l/pdb
• 分子名称: Vacuolar ATP synthase subunit C, L(+)-TARTARIC ACID (3 entities in total)
• 機能のキーワード: hydrolase, structural protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Vacuole membrane; Peripheral membrane protein: P31412
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44391.44

構造登録者

Nelson, N.,Frolow, F.,Drory, O. (登録日: 2004-08-04, 公開日: 2004-11-23, 最終更新日: 2024-03-20)

主引用文献

Drory, O.,Frolow, F.,Nelson, N.
Crystal structure of yeast V-ATPase subunit C reveals its stator function
Embo Rep., 5:1148-1152, 2004

PubMed Abstract: Vacuolar H(+)-ATPase (V-ATPase) has a crucial role in the vacuolar system of eukaryotic cells. It provides most of the energy required for transport systems that utilize the proton-motive force that is generated by ATP hydrolysis. Some, but not all, of the V-ATPase subunits are homologous to those of F-ATPase and the nonhomologous subunits determine the unique features of V-ATPase. We determined the crystal structure of V-ATPase subunit C (Vma5p), which does not show any homology with F-ATPase subunits, at 1.75 A resolution. The structural features suggest that subunit C functions as a flexible stator that holds together the catalytic and membrane sectors of the enzyme. A second crystal form that was solved at 2.9 A resolution supports the flexible nature of subunit C. These structures provide a framework for exploring the unique mechanistic features of V-ATPases.

PubMed: 15540116
DOI: 10.1038/sj.embor.7400294

実験手法

X-RAY DIFFRACTION (1.75 Å)