2O7L

The open-cap conformation of GlpG

2O7L の概要

• エントリーDOI: 10.2210/pdb2o7l/pdb
• 関連するPDBエントリー: 2IC8
• 分子名称: Protein glpG, nonyl beta-D-glucopyranoside (3 entities in total)
• 機能のキーワード: intramembrane proteolysis, rhomboid protease, glpg, membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P09391
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20548.40

構造登録者

Ha, Y. (登録日: 2006-12-11, 公開日: 2006-12-26, 最終更新日: 2023-08-30)

主引用文献

Wang, Y.,Ha, Y.
Open-cap conformation of intramembrane protease GlpG.
Proc.Natl.Acad.Sci.Usa, 104:2098-2102, 2007

PubMed Abstract: The active sites of intramembrane proteases are positioned in the lipid bilayer to facilitate peptide bond hydrolysis in the membrane. Previous crystallographic analysis of Escherichia coli GlpG, an intramembrane protease of the rhomboid family, has revealed an internal and hydrophilic active site in an apparently closed conformation. Here we describe the crystal structure of GlpG in a more open conformation, where the capping loop L5 has been lifted, exposing the previously buried and catalytically essential Ser-201 to outside aqueous solution. A water molecule now moves into the putative oxyanion hole that is constituted of a main-chain amide (Ser-201) and two conserved side chains (His-150 and Asn-154). The loop movement also destabilizes a hydrophobic side chain (Phe-245) previously buried between transmembrane helices S2 and S5 and creates a side portal from the lipid to protease active site. These results provide insights into the conformational plasticity of GlpG to accommodate substrate binding and catalysis and into the chirality of the reaction intermediate.

PubMed: 17277078
DOI: 10.1073/pnas.0611080104

実験手法

X-RAY DIFFRACTION (2.5 Å)