土拉弗朗西斯菌肽基 - tRNA水解酶的结构
Structure of Francisella tularensis peptidyl-tRNA hydrolase.
作者信息
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
机构信息
Division of Cancer Genomics and Proteomics, Ontario Cancer Institute, University Health Network, MBRC 5th Floor, 200 Elizabeth Street, Toronto, Ontario M5G 2C4, Canada.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Apr 1;67(Pt 4):446-9. doi: 10.1107/S174430911100515X. Epub 2011 Mar 26.
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.
摘要
针对细菌的新型抗生素的合理设计涉及识别参与细胞基本生化途径的酶的抑制剂。在本研究中，对兔热病病原体土拉弗朗西斯菌的肽基 - tRNA水解酶进行了克隆、表达、纯化、结晶及结构解析。土拉弗朗西斯菌肽基 - tRNA水解酶的结构与其他细菌肽基 - tRNA水解酶的结构相似，活性位点中的大多数残基在该家族中保守。所得试剂、结构数据及分析为基于结构设计此类蛋白质的新型抑制剂提供了重要信息。
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