6bnd

Crystal structure of the intrinsic colistin resistance enzyme ICR(Mc) from Moraxella catarrhalis, catalytic domain, Thr315Ala mutant mono-zinc and phosphoethanolamine complex

spinqualitylabelsall models 6bnd, resolution 1.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6bnd is a 2 chain structure with sequence from Moraxella sp. HMSC061H09. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.66Å Ligands: 15P, OPE, SO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1E9VP98_9GAMM Publication Abstract from PubMed Lipid A phosphoethanolamine (PEtN) transferases render bacteria resistant to the last resort antibiotic colistin. The recent discoveries of pathogenic bacteria harboring plasmid-borne PEtN transferase ( mcr) genes have illustrated the serious potential for wide dissemination of these resistance elements. The origin of mcr-1 is traced to Moraxella species co-occupying environmental niches with Enterobacteriaceae. Here, we describe the crystal structure of the catalytic domain of the chromosomally encoded colistin resistance PEtN transferase, ICR (Mc) (for intrinsic colistin resistance) of Moraxella catarrhalis. The ICR (Mc) structure in complex with PEtN reveals key molecular details including specific residues involved in catalysis and PEtN binding. It also demonstrates that ICR (Mc) catalytic domain dimerization is required for substrate binding. Our structure-guided phylogenetic analysis provides sequence signatures defining potentially colistin-active representatives in this enzyme family. Combined, these results advance the molecular and mechanistic understanding of PEtN transferases and illuminate their origins. Substrate Recognition by a Colistin Resistance Enzyme from Moraxella catarrhalis.,Stogios PJ, Cox G, Zubyk HL, Evdokimova E, Wawrzak Z, Wright GD, Savchenko A ACS Chem Biol. 2018 Apr 19. doi: 10.1021/acschembio.8b00116. PMID:29631403 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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