Literature summary for 2.7.6.5 extracted from

Pausch, P.; Abdelshahid, M.; Steinchen, W.; Schaefer, H.; Gratani, F.; Freibert, S.; Wolz, C.; Turgay, K.; Wilson, D.; Bange, G.
Structural basis for regulation of the opposing (p)ppGpp synthetase and hydrolase within the stringent response orchestrator rel (2020), Cell Rep., 32, 108157 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
nucleotide-free Rel has an elongated conformation in which the TGS domain contacts the synthesis domain by an interface involving alpha-helix 14 and beta strands 7/8 of the synthesis and TGS domains, respectively	Bacillus subtilis

Protein Variants

Protein Variants	Comment	Organism
E324V	inactive in (p)ppGpp synthesis	Bacillus subtilis
G283E	mutation is located at the interface of synthesis domain and TGS domain. Mutant is deregulated, showing high (p)ppGpp synthetic and reduced (p)ppGpp hydrolytic activity	Bacillus subtilis
Y279E	mutation is located at the interface of synthesis domain and TGS domain. Mutant is inactive in (p)ppGpp synthesis in vitro, but not in vivo	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	O54408	-	-
Bacillus subtilis 168	O54408	-	-

Synonyms

Synonyms	Comment	Organism
RelA	-	Bacillus subtilis

General Information

General Information	Comment	Organism
physiological function	the Rel holoenzyme consists of the N-terminal hydrolase and synthetase domains, followed by its regulatory C-terminal domain consisting of the TGS, AH, RIS, and ACT domains. Removal of the TGS and AH subdomains leads to a pronounced increase in (p)ppGpp synthesis and a corresponding decrease in (p)ppGpp hydrolysis. Rel forms homodimers, which appear to control the interaction with deacylated-tRNA, but not the enzymatic activity of Rel	Bacillus subtilis

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Release 2023.1 (January 2023)