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Atomic structure of and valine binding to the regulatory ACT domain of the Mycobacterium tuberculosis Rel protein
Author(s) -
Shin Joon,
Singal Bharti,
Sony Subramanian Manimekalai Malathy,
Wei Chen Ming,
Ragunathan Priya,
Grüber Gerhard
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15600
Subject(s) - valine , stringent response , mycobacterium tuberculosis , amino acid , biochemistry , protein data bank (rcsb pdb) , hydrolase , biology , ribosome , chemistry , stereochemistry , mutant , enzyme , gene , rna , medicine , tuberculosis , pathology
The stringent response (SR) is crucial for survival as well as optimal growth of Mycobacterium tuberculosis (Mtb) . Mycobacterial cells initiate SR during nutrient and energy limitations by increasing levels of (p)ppGpp. In Mtb , (p)ppGpp synthesis and degradation are carried out by the bifunctional enzyme Rel. Here, we present the dimeric solution structure of its ACT domain, unraveled its specific binding to valine, and determined the critical residues in Val‐ACT binding.