2BL2

The membrane rotor of the V-type ATPase from Enterococcus hirae

2BL2 の概要

• エントリーDOI: 10.2210/pdb2bl2/pdb
• 分子名称: V-TYPE SODIUM ATP SYNTHASE SUBUNIT K, 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: v-type atpase, k-ring, membrane rotor, sodium transporter, hydrogen ion transport, hydrolase, transmembrane
• 由来する生物種: ENTEROCOCCUS HIRAE
• 細胞内の位置: Cell membrane; Multi-pass membrane protein (Potential): P43457
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 207742.54

構造登録者

Murata, T.,Yamato, I.,Kakinuma, Y.,Leslie, A.G.W.,Walker, J.E. (登録日: 2005-02-25, 公開日: 2005-04-05, 最終更新日: 2024-05-08)

主引用文献

Murata, T.,Yamato, I.,Kakinuma, Y.,Leslie, A.G.W.,Walker, J.E.
Structure of the Rotor of the Vacuolar-Type Na- ATPase from Enterococcus Hirae
Science, 308:654-, 2005

PubMed Abstract: The membrane rotor ring from the vacuolar-type (V-type) sodium ion-pumping adenosine triphosphatase (Na+-ATPase) from Enterococcus hirae consists of 10 NtpK subunits, which are homologs of the 16-kilodalton and 8-kilodalton proteolipids found in other V-ATPases and in F1Fo- or F-ATPases, respectively. Each NtpK subunit has four transmembrane alpha helices, with a sodium ion bound between helices 2 and 4 at a site buried deeply in the membrane that includes the essential residue glutamate-139. This site is probably connected to the membrane surface by two half-channels in subunit NtpI, against which the ring rotates. Symmetry mismatch between the rotor and catalytic domains appears to be an intrinsic feature of both V- and F-ATPases.

PubMed: 15802565
DOI: 10.1126/SCIENCE.1110064

実験手法

X-RAY DIFFRACTION (2.1 Å)