Structure of Francisella tularensis peptidyl-tRNA hydrolase

被引：21

作者：

Clarke, Teresa E. ^{[1
,2
]}

Romanov, Vladimir ^{[1
,2
]}

Lam, Robert ^{[1
,2
]}

Gothe, Scott A. ^{[3
]}

Peddi, Srinivasa R. ^{[3
]}

Razumova, Ekaterina B. ^{[2
]}

Lipman, Richard S. A. ^{[3
]}

Branstrom, Arthur A. ^{[3
]}

Chirgadze, Nickolay Y. ^{[1
,2
,4
]}

机构：

[1] Ontario Canc Inst, Univ Hlth Network, Div Canc Genom & Prote, Toronto, ON M5G 2C4, Canada

[2] NEXTEX Technol Inc, Toronto, ON M4N 1W6, Canada

[3] PTC Therapeut Inc, S Plainfield, NJ 07080 USA

[4] Univ Toronto, Dept Pharmacol & Toxicol, Toronto, ON M5S 1A8, Canada

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2011年 / 67卷

关键词：

peptidyl-tRNA hydrolases; Francisella tularensis; CRYSTAL-STRUCTURE; ANGSTROM RESOLUTION; METABOLIC ROLE; PROTEIN; ENZYME;

D O I：

10.1107/S174430911100515X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：446 / 449

页数：4

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