title: Structure of Francisella tularensis peptidyl-tRNA hydrolase.
abstract: 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.
authors.affiliation: Division of Cancer Genomics and Proteomics, Ontario Cancer Institute, University Health Network, MBRC 5th Floor, 200 Elizabeth Street, Toronto, Ontario M5G 2C4, Canada.
authors.forename: Teresa E
authors.initials: TE
authors.lastname: Clarke
authors.forename: Vladimir
authors.initials: V
authors.lastname: Romanov
authors.forename: Robert
authors.initials: R
authors.lastname: Lam
authors.forename: Scott A
authors.initials: SA
authors.lastname: Gothe
authors.forename: Srinivasa R
authors.initials: SR
authors.lastname: Peddi
authors.forename: Ekaterina B
authors.initials: EB
authors.lastname: Razumova
authors.forename: Richard S A
authors.initials: RS
authors.lastname: Lipman
authors.forename: Arthur A
authors.initials: AA
authors.lastname: Branstrom
authors.forename: Nickolay Y
authors.initials: NY
authors.lastname: Chirgadze
mesh_terms: D002265:Carboxylic Ester Hydrolases / Q000737:chemistry*; D018360:Crystallography, X-Ray; D005604:Francisella tularensis / Q000201:enzymology*; D008958:Models, Molecular; D017434:Protein Structure, Tertiary
chemical_list: D002265:Carboxylic Ester Hydrolases; C019674:aminoacyl-tRNA hydrolase