2o7l

The open-cap conformation of GlpG

spinqualitylabelsall models 2o7l, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2o7l is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. Ligands: BNG Related: 2ic8 Gene: glpG ("Bacillus coli" Migula 1895) Activity: Glucokinase, with EC number 2.7.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum 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 The active sites of intramembrane proteases are positioned in the lipid bilayer to facilitate peptide bond hydrolysis in the membrane. Previous crystallographic analysis of Escherichia coli GlpG, an intramembrane protease of the rhomboid family, has revealed an internal and hydrophilic active site in an apparently closed conformation. Here we describe the crystal structure of GlpG in a more open conformation, where the capping loop L5 has been lifted, exposing the previously buried and catalytically essential Ser-201 to outside aqueous solution. A water molecule now moves into the putative oxyanion hole that is constituted of a main-chain amide (Ser-201) and two conserved side chains (His-150 and Asn-154). The loop movement also destabilizes a hydrophobic side chain (Phe-245) previously buried between transmembrane helices S2 and S5 and creates a side portal from the lipid to protease active site. These results provide insights into the conformational plasticity of GlpG to accommodate substrate binding and catalysis and into the chirality of the reaction intermediate. Open-cap conformation of intramembrane protease GlpG.,Wang Y, Ha Y Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2098-102. Epub 2007 Feb 2. PMID:17277078 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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