2GQC

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

Summary for 2GQC

• Entry DOI: 10.2210/pdb2gqc/pdb
• Descriptor: Rhomboid Intramembrane Protease (1 entity in total)
• Functional Keywords: alpha-beta domain, hydrolase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 7941.02

Authors

Dutta, K.,Del Rio, A.,Chavez, J.,Ubarretxena-Belandia, I.,Ghose, R. (deposition date: 2006-04-20, release date: 2007-03-06, Last modification date: 2024-05-01)

Primary citation

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

Experimental method

SOLUTION NMR