2IRV

Crystal structure of GlpG, a rhomboid intramembrane serine protease

2IRV の概要

• エントリーDOI: 10.2210/pdb2irv/pdb
• 関連するPDBエントリー: 2IC8
• 分子名称: Protein glpG, LAURYL DIMETHYLAMINE-N-OXIDE, PHOSPHATE ION, ... (6 entities in total)
• 機能のキーワード: membrane protein, cavity, ser-his dyad
• 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: 2
• 化学式量合計: 48384.83

構造登録者

Bibi, E.,Fass, D.,Ben-Shem, A. (登録日: 2006-10-16, 公開日: 2006-10-31, 最終更新日: 2024-02-21)

主引用文献

Ben-Shem, A.,Fass, D.,Bibi, E.
Structural basis for intramembrane proteolysis by rhomboid serine proteases.
Proc.Natl.Acad.Sci.Usa, 104:462-466, 2007

PubMed Abstract: Intramembrane proteases catalyze peptide bond cleavage of integral membrane protein substrates. This activity is crucial for many biological and pathological processes. Rhomboids are evolutionarily widespread intramembrane serine proteases. Here, we present the 2.3-A-resolution crystal structure of a rhomboid from Escherichia coli. The enzyme has six transmembrane helices, five of which surround a short TM4, which starts deep within the membrane at the catalytic serine residue. Thus, the catalytic serine is in an externally exposed cavity, which provides a hydrophilic environment for proteolysis. Our results reveal a mechanism to enable water-dependent catalysis at the depth of the hydrophobic milieu of the membrane and suggest how substrates gain access to the sequestered rhomboid active site.

PubMed: 17190827
DOI: 10.1073/pnas.0609773104

実験手法

X-RAY DIFFRACTION (2.3 Å)