2nr9

Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae

spinqualitylabelsall models 2nr9, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2nr9 is a 1 chain structure with sequence from Haemophilus influenzae 86-028NP. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: PA6, PQE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLPG_HAEIN Rhomboid-type serine protease that catalyzes intramembrane proteolysis (By similarity). 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 PubMed Rhomboid peptidases are members of a family of regulated intramembrane peptidases that cleave the transmembrane segments of integral membrane proteins. Rhomboid peptidases have been shown to play a major role in developmental processes in Drosophila and in mitochondrial maintenance in yeast. Most recently, the function of rhomboid peptidases has been directly linked to apoptosis. We have solved the structure of the rhomboid peptidase from Haemophilus influenzae (hiGlpG) to 2.2-A resolution. The phasing for the crystals of hiGlpG was provided mainly by molecular replacement, by using the coordinates of the Escherichia coli rhomboid (ecGlpG). The structural results on these rhomboid peptidases have allowed us to speculate on the catalytic mechanism of substrate cleavage in a membranous environment. We have identified the relative disposition of the nucleophilic serine to the general base/acid function of the conserved histidine. Modeling a tetrapeptide substrate in the context of the rhomboid structure reveals an oxyanion hole comprising the side chain of a second conserved histidine and the main-chain NH of the nucleophilic serine residue. In both hiGlpG and ecGlpG structures, a water molecule occupies this oxyanion hole. The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis.,Lemieux MJ, Fischer SJ, Cherney MM, Bateman KS, James MN Proc Natl Acad Sci U S A. 2007 Jan 16;104(3):750-4. Epub 2007 Jan 8. PMID:17210913 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Rhomboid protease

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