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Literature summary extracted from

  • Stogios, P.J.; Cox, G.; Zubyk, H.L.; Evdokimova, E.; Wawrzak, Z.; Wright, G.D.; Savchenko, A.
    Substrate recognition by a colistin resistance enzyme from Moraxella catarrhalis (2018), ACS Chem. Biol., 13, 1322-1332 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.8.43 structure of the catalytic domain of ICR.. Catalytic domain dimerization is required for substrate binding. The structure reveals two disulfide bonds (Cys390 to Cys398, Cys448 to Cys456) Moraxella sp. HMSC061H09

Protein Variants

EC Number Protein Variants Comment Organism
2.7.8.43 T315A mutation of the catalytic domain, abolishes antibiotic resistance activity Moraxella sp. HMSC061H09

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.8.43 Zn2+ a single Zn2+ atom is bound to ICR active site Moraxella sp. HMSC061H09

Organism

EC Number Organism UniProt Comment Textmining
2.7.8.43 Moraxella sp. HMSC061H09 A0A1E9VP98
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Synonyms

EC Number Synonyms Comment Organism
2.7.8.43 colistin resistance PEtN transferase
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 Moraxella sp. HMSC061H09
2.7.8.43 HMPREF2573_04170
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 Moraxella sp. HMSC061H09
2.7.8.43 ICR
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 Moraxella sp. HMSC061H09
2.7.8.43 intrinsic colistin resistance enzyme
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 Moraxella sp. HMSC061H09

General Information

EC Number General Information Comment Organism
2.7.8.43 physiological function expression in Escherichia coli leads to 4fold increase in resistance to antibiotics colistin and polymyxin B. In addition to the catalytoc domain, the N-terminal transmembrane regions are required to confer drug resistance in the cell Moraxella sp. HMSC061H09