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Literature summary for 3.4.21.92 extracted from

  • Choules, M.P.; Wolf, N.M.; Lee, H.; Anderson, J.R.; Grzelak, E.M.; Wang, Y.; Ma, R.; Gao, W.; McAlpine, J.B.; Jin, Y.Y.; Cheng, J.; Lee, H.; Suh, J.W.; Duc, N.M.; Paik, S.; Choe, J.H.; Jo, E.K.; Chang, C.L.; Lee, J.S.; Jaki, B.U.; Pauli, G.F.; Franzblau, S.G.; Cho, S.
    Rufomycin targets ClpC1 proteolysis in Mycobacterium tuberculosis and M. abscessus (2019), Antimicrob. Agents Chemother., 63, e02204 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information spontaneously generated mutants resistant to rufomycin I involve seven unique single nucleotide polymorphism mutations at three distinct codons within the N-terminal domain of clpC1 (V13, H77, and F80) Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
rufomycin I cyclic peptide with potent and selective in vitro activity against Mycobacterium tuberculosis and Mycobacterium abscessus. Compound significantly decreases the proteolytic capabilities of the ClpC1/P1/P2 complex to degrade casein, while having no significant effect on the ATPase activity of ClpC1 Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WPC5 and P9WPC3 P9WPC5 i.e. subunit P1, P9WPC3 i.e. subunit P2
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Mycobacterium tuberculosis H37Rv P9WPC5 and P9WPC3 P9WPC5 i.e. subunit P1, P9WPC3 i.e. subunit P2
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