2gqc: Difference between revisions
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|ACTIVITY= [http://en.wikipedia.org/wiki/Rhomboid_protease Rhomboid protease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.105 3.4.21.105] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Rhomboid_protease Rhomboid protease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.105 3.4.21.105] </span> | ||
|GENE= | |GENE= | ||
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gqc OCA], [http://www.ebi.ac.uk/pdbsum/2gqc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gqc RCSB]</span> | |||
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[[Category: alpha-beta domain]] | [[Category: alpha-beta domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:20:05 2008'' | ||
Revision as of 03:20, 31 March 2008
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| Activity: | Rhomboid protease, with EC number 3.4.21.105 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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