3nea

Crystal Structure of Peptidyl-tRNA hydrolase from Francisella tularensisCrystal Structure of Peptidyl-tRNA hydrolase from Francisella tularensis

Structural highlights 3nea is a 1 chain structure with sequence from Francisella tularensis subsp. tularensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.25Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PTH_FRATT The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity). Publication Abstract from PubMed The rational design of novel antibiotics for bacteria involves the identification of inhibitors for enzymes involved in essential biochemical pathways in cells. In this study, the cloning, expression, purification, crystallization and structure of the enzyme peptidyl-tRNA hydrolase from Francisella tularensis, the causative agent of tularemia, was performed. The structure of F. tularensis peptidyl-tRNA hydrolase is comparable to those of other bacterial peptidyl-tRNA hydrolases, with most residues in the active site conserved amongst the family. The resultant reagents, structural data and analyses provide essential information for the structure-based design of novel inhibitors for this class of proteins. Structure of Francisella tularensis peptidyl-tRNA hydrolase.,Clarke TE, Romanov V, Lam R, Gothe SA, Peddi SR, Razumova EB, Lipman RS, Branstrom AA, Chirgadze NY Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Apr 1;67(Pt, 4):446-9. Epub 2011 Mar 26. PMID:21505237 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Peptidyl-tRNA hydrolase

spinqualitylabelsall models 3nea, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image