2NR9

Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae

2NR9 の概要

• エントリーDOI: 10.2210/pdb2nr9/pdb
• 関連するPDBエントリー: 2IC8
• 分子名称: Protein glpG homolog, (R)-2-(FORMYLOXY)-3-(PHOSPHONOOXY)PROPYL PENTANOATE, 3,6,12,15,18,21,24-HEPTAOXAHEXATRIACONTAN-1-OL, ... (4 entities in total)
• 機能のキーワード: intramembrane peptidase, rhomboid protease, membrane protein
• 由来する生物種: Haemophilus influenzae
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P44783
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24067.08

構造登録者

Lemieux, M.J.,Fischer, S.J.,Cherney, M.M.,Bateman, K.S.,James, M.N.G. (登録日: 2006-11-01, 公開日: 2006-11-14, 最終更新日: 2023-08-30)

主引用文献

Lemieux, M.J.,Fischer, S.J.,Cherney, M.M.,Bateman, K.S.,James, M.N.G.
The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis.
Proc.Natl.Acad.Sci.USA, 104:750-754, 2007

PubMed Abstract: Rhomboid peptidases are members of a family of regulated intramembrane peptidases that cleave the transmembrane segments of integral membrane proteins. Rhomboid peptidases have been shown to play a major role in developmental processes in Drosophila and in mitochondrial maintenance in yeast. Most recently, the function of rhomboid peptidases has been directly linked to apoptosis. We have solved the structure of the rhomboid peptidase from Haemophilus influenzae (hiGlpG) to 2.2-A resolution. The phasing for the crystals of hiGlpG was provided mainly by molecular replacement, by using the coordinates of the Escherichia coli rhomboid (ecGlpG). The structural results on these rhomboid peptidases have allowed us to speculate on the catalytic mechanism of substrate cleavage in a membranous environment. We have identified the relative disposition of the nucleophilic serine to the general base/acid function of the conserved histidine. Modeling a tetrapeptide substrate in the context of the rhomboid structure reveals an oxyanion hole comprising the side chain of a second conserved histidine and the main-chain NH of the nucleophilic serine residue. In both hiGlpG and ecGlpG structures, a water molecule occupies this oxyanion hole.

PubMed: 17210913
DOI: 10.1073/pnas.0609981104

実験手法

X-RAY DIFFRACTION (2.2 Å)