4PX7

Crystal structure of lipid phosphatase E. coli PgpB

4PX7 の概要

• エントリーDOI: 10.2210/pdb4px7/pdb
• 関連するPDBエントリー: 1EOI
• 分子名称: Phosphatidylglycerophosphatase, LAURYL DIMETHYLAMINE-N-OXIDE, GLYCEROL (3 entities in total)
• 機能のキーワード: helix, alfa-helix, hydrolase, membrane
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30626.27

構造登録者

Fan, J.,Jiang, D.,Zhao, Y.,Zhang, X.C. (登録日: 2014-03-22, 公開日: 2014-05-28, 最終更新日: 2024-10-30)

主引用文献

Fan, J.,Jiang, D.,Zhao, Y.,Liu, J.,Zhang, X.C.
Crystal structure of lipid phosphatase Escherichia coli phosphatidylglycerophosphate phosphatase B.
Proc.Natl.Acad.Sci.USA, 111:7636-7640, 2014

PubMed Abstract: Membrane-integrated type II phosphatidic acid phosphatases (PAP2s) are important for numerous bacterial to human biological processes, including glucose transport, lipid metabolism, and signaling. Escherichia coli phosphatidylglycerol-phosphate phosphatase B (ecPgpB) catalyzes removing the terminal phosphate group from a lipid carrier, undecaprenyl pyrophosphate, and is essential for transport of many hydrophilic small molecules across the membrane. We determined the crystal structure of ecPgpB at a resolution of 3.2 Å. This structure shares a similar folding topology and a nearly identical active site with soluble PAP2 enzymes. However, the substrate binding mechanism appears to be fundamentally different from that in soluble PAP2 enzymes. In ecPgpB, the potential substrate entrance to the active site is located in a cleft formed by a V-shaped transmembrane helix pair, allowing lateral movement of the lipid substrate entering the active site from the membrane lipid bilayer. Activity assays of point mutations confirmed the importance of the catalytic residues and potential residues involved in phosphate binding. The structure also suggests an induced-fit mechanism for the substrate binding. The 3D structure of ecPgpB serves as a prototype to study eukaryotic PAP2 enzymes, including human glucose-6-phosphatase, a key enzyme in the homeostatic regulation of blood glucose concentrations.

PubMed: 24821770
DOI: 10.1073/pnas.1403097111

実験手法

X-RAY DIFFRACTION (3.2 Å)