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Literature summary 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 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.92 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

EC Number Organism UniProt Comment Textmining
3.4.21.92 Mycobacterium tuberculosis
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General Information

EC Number General Information Comment Organism
3.4.21.92 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