1t7d | pdb_00001t7d

Crystal structure of Escherichia coli type I signal peptidase in complex with a lipopeptide inhibitor

spinqualitylabelsall models 1t7d, resolution 2.47Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1t7d is a 4 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895 and Chainia sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: M12 NonStd Res: 5PG, DAL, DSE Related: 1b12, 1kn9, 3iiq Gene: LEPB ("Bacillus coli" Migula 1895) Activity: Signal peptidase I, with EC number 3.4.21.89 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 We report here the crystallographic and biophysical analysis of a soluble, catalytically active fragment of the Escherichia coli type I signal peptidase (SPase Delta2-75) in complex with arylomycin A2. The 2.5-A resolution structure revealed that the inhibitor is positioned with its COOH-terminal carboxylate oxygen (O45) within hydrogen bonding distance of all the functional groups in the catalytic center of the enzyme (Ser90 O-gamma, Lys145 N-zeta, and Ser88 O-gamma) and that it makes beta-sheet type interactions with the beta-strands that line each side of the binding site. Ligand binding studies, calorimetry, fluorescence spectroscopy, and stopped-flow kinetics were also used to analyze the binding mode of this unique non-covalently bound inhibitor. The crystal structure was solved in the space group P4(3)2(1)2. A detailed comparison is made to the previously published acyl-enzyme inhibitor complex structure (space group: P2(1)2(1)2) and the apo-enzyme structure (space group: P4(1)2(1)2). Together this work provides insights into the binding of pre-protein substrates to signal peptidase and will prove helpful in the development of novel antibiotics. Crystallographic and biophysical analysis of a bacterial signal peptidase in complex with a lipopeptide-based inhibitor.,Paetzel M, Goodall JJ, Kania M, Dalbey RE, Page MG J Biol Chem. 2004 Jul 16;279(29):30781-90. Epub 2004 May 10. PMID:15136583 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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