4AV3

Crystal structure of Thermotoga Maritima sodium pumping membrane integral pyrophosphatase with metal ions in active site

4AV3 の概要

• エントリーDOI: 10.2210/pdb4av3/pdb
• 関連するPDBエントリー: 4AV6
• 分子名称: K(+)-STIMULATED PYROPHOSPHATE-ENERGIZED SODIUM PUMP, MAGNESIUM ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, membrane pyrophosphotase, ion pump
• 由来する生物種: THERMOTOGA MARITIMA
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : Q9S5X0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 156563.05

構造登録者

Kajander, T.,Kogan, K.,Kellosalo, J.,Pokharel, K.,Goldman, A. (登録日: 2012-05-23, 公開日: 2012-08-08, 最終更新日: 2024-05-01)

主引用文献

Kellosalo, J.,Kajander, T.,Kogan, K.,Pokharel, K.,Goldman, A.
The Structure and Catalytic Cycle of a Sodium-Pumping Pyrophosphatase.
Science, 337:473-, 2012

PubMed Abstract: Membrane-integral pyrophosphatases (M-PPases) are crucial for the survival of plants, bacteria, and protozoan parasites. They couple pyrophosphate hydrolysis or synthesis to Na(+) or H(+) pumping. The 2.6-angstrom structure of Thermotoga maritima M-PPase in the resting state reveals a previously unknown solution for ion pumping. The hydrolytic center, 20 angstroms above the membrane, is coupled to the gate formed by the conserved Asp(243), Glu(246), and Lys(707) by an unusual "coupling funnel" of six α helices. Comparison with our 4.0-angstrom resolution structure of the product complex suggests that helix 12 slides down upon substrate binding to open the gate by a simple binding-change mechanism. Below the gate, four helices form the exit channel. Superimposing helices 3 to 6, 9 to 12, and 13 to 16 suggests that M-PPases arose through gene triplication.

PubMed: 22837527
DOI: 10.1126/SCIENCE.1222505

実験手法

X-RAY DIFFRACTION (2.6 Å)