2gqc: Difference between revisions
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==Solution structure of the N-terminal domain of Rhomboid Intramembrane Protease from P. aeruginosa== | ==Solution structure of the N-terminal domain of Rhomboid Intramembrane Protease from P. aeruginosa== | ||
<StructureSection load='2gqc' size='340' side='right' caption='[[2gqc]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2gqc' size='340' side='right'caption='[[2gqc]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2gqc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GQC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GQC FirstGlance]. <br> | <table><tr><td colspan='2'>[[2gqc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GQC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GQC FirstGlance]. <br> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Pseae]] | [[Category: Pseae]] | ||
[[Category: Rhomboid protease]] | [[Category: Rhomboid protease]] | ||
Revision as of 14:18, 27 March 2020
Solution structure of the N-terminal domain of Rhomboid Intramembrane Protease from P. aeruginosaSolution structure of the N-terminal domain of Rhomboid Intramembrane Protease from P. aeruginosa
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedRhomboids 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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