2IC8

Crystal structure of GlpG

2IC8 の概要

• エントリーDOI: 10.2210/pdb2ic8/pdb
• 分子名称: Protein glpG, nonyl beta-D-glucopyranoside (3 entities in total)
• 機能のキーワード: rhomboid, intramembrane proteolysis, 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: 24205.05

構造登録者

Ha, Y. (登録日: 2006-09-12, 公開日: 2006-10-17, 最終更新日: 2024-02-21)

主引用文献

Wang, Y.,Zhang, Y.,Ha, Y.
Crystal structure of a rhomboid family intramembrane protease.
Nature, 444:179-180, 2006

PubMed Abstract: Escherichia coli GlpG is an integral membrane protein that belongs to the widespread rhomboid protease family. Rhomboid proteases, like site-2 protease (S2P) and gamma-secretase, are unique in that they cleave the transmembrane domain of other membrane proteins. Here we describe the 2.1 A resolution crystal structure of the GlpG core domain. This structure contains six transmembrane segments. Residues previously shown to be involved in catalysis, including a Ser-His dyad, and several water molecules are found at the protein interior at a depth below the membrane surface. This putative active site is accessible by substrate through a large 'V-shaped' opening that faces laterally towards the lipid, but is blocked by a half-submerged loop structure. These observations indicate that, in intramembrane proteolysis, the scission of peptide bonds takes place within the hydrophobic environment of the membrane bilayer. The crystal structure also suggests a gating mechanism for GlpG that controls substrate access to its hydrophilic active site.

PubMed: 17051161
DOI: 10.1038/nature05255

実験手法

X-RAY DIFFRACTION (2.1 Å)