2GQC

Solution structure of the N-terminal domain of Rhomboid Intramembrane Protease from P. aeruginosa

2GQC の概要

• エントリーDOI: 10.2210/pdb2gqc/pdb
• 分子名称: Rhomboid Intramembrane Protease (1 entity in total)
• 機能のキーワード: alpha-beta domain, hydrolase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7941.02

構造登録者

Dutta, K.,Del Rio, A.,Chavez, J.,Ubarretxena-Belandia, I.,Ghose, R. (登録日: 2006-04-20, 公開日: 2007-03-06, 最終更新日: 2024-05-01)

主引用文献

Del Rio, A.,Dutta, K.,Chavez, J.,Ubarretxena-Belandia, I.,Ghose, R.
Solution structure and dynamics of the N-terminal cytosolic domain of rhomboid intramembrane protease from Pseudomonas aeruginosa: insights into a functional role in intramembrane proteolysis.
J.Mol.Biol., 365:109-122, 2007

PubMed Abstract: Rhomboids are ubiquitous integral membrane proteases that release cellular signals from membrane-bound substrates through a general signal transduction mechanism known as regulated intramembrane proteolysis (RIP). We present the NMR structure of the cytosolic N-terminal domain (NRho) of P. aeruginosa Rhomboid. NRho consists of a novel alpha/beta fold and represents the first detailed structural insight into this class of intramembrane proteases. We find evidence that NRho is capable of strong and specific association with detergent micelles that mimic the membrane/water interface. Relaxation measurements on NRho reveal structural fluctuations on the microseconds-milliseconds timescale in regions including and contiguous to those implicated in membrane interaction. This structural plasticity may facilitate the ability of NRho to recognize and associate with membranes. We suggest that NRho plays a role in scissile peptide bond selectivity by optimally positioning the Rhomboid active site relative to the membrane plane.

PubMed: 17059825
DOI: 10.1016/j.jmb.2006.09.047

実験手法

SOLUTION NMR