Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Clarke TE, Romanov V, Lam R, Gothe SA, Peddi SR, Razumova EB, Lipman RS, Branstrom AA, Chirgadze NY. Structure of Francisella tularensis peptidyl-tRNA hydrolase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Apr 1;67(Pt, 4):446-9. Epub 2011 Mar 26. PMID:21505237 doi:10.1107/S174430911100515X
