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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Apr 1;67(Pt 4):446-9. doi: 10.1107/S174430911100515X. Epub 2011 Mar 26.

Structure of Francisella tularensis peptidyl-tRNA hydrolase.

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1
Division of Cancer Genomics and Proteomics, Ontario Cancer Institute, University Health Network, MBRC 5th Floor, 200 Elizabeth Street, Toronto, Ontario M5G 2C4, Canada.

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.

PMID:
21505237
PMCID:
PMC3080146
DOI:
10.1107/S174430911100515X
[Indexed for MEDLINE]
Free PMC Article
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