Structural highlights
Function[D0ZJ57_SALT1] The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity).[HAMAP-Rule:MF_00083] Publication Abstract from PubMedPeptidyl-tRNA hydrolase (Pth; EC 3.1.1.29) from the pathogenic bacterium Salmonella typhimurium has been cloned, expressed in Escherichia coli and crystallized for X-ray analysis. Crystals were grown using hanging-drop vapor diffusion against a reservoir solution consisting of 0.03 M citric acid, 0.05 M bis-tris propane, 1% glycerol, 3% sucrose, 25% PEG 6000 pH 7.6. Crystals were used to obtain the three-dimensional structure of the native protein at 1.6 A resolution. The structure was determined by molecular replacement of the crystallographic data processed in space group P2(1)2(1)2(1) with unit-cell parameters a=62.1, b=64.9, c=110.5 A, alpha=beta=gamma=90 degrees . The asymmetric unit of the crystallographic lattice was composed of two copies of the enzyme molecule with a 51% solvent fraction, corresponding to a Matthews coefficient of 2.02 A3 Da(-1). The structural coordinates reported serve as a foundation for computational and structure-guided efforts towards novel small-molecule Pth1 inhibitors and potential antibacterial development. Recombinant production, crystallization and X-ray crystallographic structure determination of peptidyl-tRNA hydrolase from Salmonella typhimurium.,Vandavasi V, Taylor-Creel K, McFeeters RL, Coates L, McFeeters H Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):872-7. doi:, 10.1107/S2053230X14009893. Epub 2014 Jun 18. PMID:25005080[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 05:08, 25 December 2014.