Structure of Francisella tularensis peptidyl-tRNA hydrolase

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...

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Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2011-04, Vol.67 (4), p.446-449
Main Authors: Clarke, Teresa E., Romanov, Vladimir, Lam, Robert, Gothe, Scott A., Peddi, Srinivasa R., Razumova, Ekaterina B., Lipman, Richard S. A., Branstrom, Arthur A., Chirgadze, Nickolay Y.
Format: Article
Language:English
Subjects:
Antibiotics
Bacteriology
Carboxylic Ester Hydrolases - chemistry
Cloning
Crystallization
Crystallography, X-Ray
Francisella tularensis
Francisella tularensis - enzymology
Inhibitors
Models, Molecular
Mutation
peptidyl-tRNA hydrolases
Protein Structure, Tertiary
Reagents
Structural Communications
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Summary: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.
ISSN:1744-3091
1744-3091
2053-230X
DOI:10.1107/S174430911100515X