2gqc: Difference between revisions

Revision as of 18:34, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

2GQC is a Single protein structure of sequence from Pseudomonas aeruginosa pao1. Active as Rhomboid protease, with EC number 3.4.21.105 Full crystallographic information is available from OCA.

ReferenceReference

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., Del Rio A, Dutta K, Chavez J, Ubarretxena-Belandia I, Ghose R, J Mol Biol. 2007 Jan 5;365(1):109-22. Epub 2006 Sep 23. PMID:17059825

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OCA

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 ==Overview==
-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.
+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.
 ==About this Structure==
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 [[Category: Dutta, K.]]
 [[Category: Ghose, R.]]
-[[Category: Rio, A.Del.]]
+[[Category: Rio, A Del.]]
 [[Category: Ubarretxena-Belandia, I.]]
 [[Category: alpha-beta domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:05:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:34:13 2008''