Atomic structure of the regulatory TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA

被引:4
作者
Shin, Joon [1 ]
Singal, Bharti [1 ]
Gruber, Ardina [1 ]
Wong, David Meng Kit [1 ]
Ragunathan, Priya [1 ]
Gruber, Gerhard [1 ]
机构
[1] Nanyang Technol Univ, Sch Biol Sci, Singapore 637551, Singapore
关键词
Mycobacterium tuberculosis; NMR spectroscopy; Rel; stringent response; TGS domain; tuberculosis; STRINGENT RESPONSE; SPOT HOMOLOG; PPGPP; CRYSTALLOGRAPHY; ACTIVATION; STARVATION; REL(MTB); SYSTEM; ENZYME;
D O I
10.1002/1873-3468.14236
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
The stringent response is critical for the survival of Mycobacterium tuberculosis (Mtb) under nutrient starvation. The mechanism is mediated by a GTP pyrophosphokinase known as Rel, containing N-terminal synthetase and hydrolase domains and C-terminal regulatory domains, which include the TGS domain (ThrRS, GTPase, and SpoT proteins) that has been proposed to activate the synthetase domain via interaction with deacylated tRNA. Here, we present the NMR solution structure of the Mtb Rel TGS domain (MtRel TGS), consisting of five antiparallel beta-strands and one helix-loop-helix motif. The interaction of MtRel TGS with deacylated tRNA is shown, indicating the critical amino acids of MtRel TGS in tRNA binding, and presenting the first structural evidence of MtRel TGS binding to deacylated tRNA in solution in the absence of the translational machinery.
引用
收藏
页码:3006 / 3018
页数:13
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