Literature summary for 3.4.21.92 extracted from

Weinhaeupl, K.; Brennich, M.; Kazmaier, U.; Lelievre, J.; Ballell, L.; Goldberg, A.; Schanda, P.; Fraga, H.
The antibiotic cyclomarin blocks arginine-phosphate-induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis (2018), J. Biol. Chem., 293, 8379-8393 .

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Inhibitors

Inhibitors	Comment	Organism	Structure
cyclomarin	cyclomarin binding to subunit ClpC1 N-terminal domain specifically blockes the N-terminal dynamics induced by arginine-phosphate binding. Cyclomarin-induced restriction of ClpC1 dynamics may modulate the chaperone enzymatic activity leading eventually to cell death	Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	-	-	-

General Information

General Information	Comment	Organism
physiological function	arginine-phosphate and arginine-phosphorylated proteins bind to subunit ClpC1 N-terminal domain and induce millisecond dynamics. These dynamics are caused by conformational changes and do not result from unfolding or oligomerization of this domain	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)