The crystal structure of the catalytic domain of the ser/thr kinase PknA from M. tuberculosis shows an Src-like autoinhibited conformation

被引：10
|
作者：
Wagner, Tristan [1 ,2 ,3 ]
Alexandre, Matthieu [1 ,2 ,3 ]
Duran, Rosario [4 ,5 ]
Barilone, Nathalie [1 ,2 ,3 ]
Wehenkel, Annemarie [1 ,2 ,3 ]
Alzari, Pedro M. [1 ,2 ,3 ]
Bellinzoni, Marco [1 ,2 ,3 ]
机构：
[1] Inst Pasteur, Unite Microbiol Struct, F-75724 Paris, France
[2] CNRS, UMR 3528, F-75724 Paris, France
[3] Univ Paris Diderot, Sorbonne Paris Cite, Microbiol Struct, F-75724 Paris, France
[4] Inst Pasteur Montevideo, Unidad Bioquim & Proteom Analit, Montevideo, Uruguay
[5] Minist Educ & Cultura, Unidad Bioquim & Proteom Analit, Inst Invest Biol Clemente Estable, Montevideo, Uruguay
来源：
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2015年 / 83卷 / 05期
关键词：
Mycobacterium tuberculosis; Ser; Thr phosphorylation; autophosphorylation; autoinhibition; X-ray crystallography; mass spectrometry; MYCOBACTERIUM-TUBERCULOSIS; PROTEIN-KINASE; REFINEMENT; MECHANISM; FEATURES; RECEPTOR;
D O I：
10.1002/prot.24754
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Signal transduction mediated by Ser/Thr phosphorylation in Mycobacterium tuberculosis has been intensively studied in the last years, as its genome harbors eleven genes coding for eukaryotic-like Ser/Thr kinases. Here we describe the crystal structure and the autophosphorylation sites of the catalytic domain of PknA, one of two protein kinases essential for pathogen's survival. The structure of the ligand-free kinase domain shows an auto-inhibited conformation similar to that observed in human Tyr kinases of the Src-family. These results reinforce the high conservation of structural hallmarks and regulation mechanisms between prokaryotic and eukaryotic protein kinases. Proteins 2015; 83:982-988. (c) 2015 Wiley Periodicals, Inc.
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收藏
页码：982 / 988
页数：7
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