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PDBsum entry 6bnc
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PDB id:
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Transferase
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Title:
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Crystal structure of the intrinsic colistin resistance enzyme icr(mc) from moraxella catarrhalis, catalytic domain, thr315ala mutant di- zinc and peg complex
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Structure:
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Phosphoethanolamine transferase. Chain: a, b. Engineered: yes. Mutation: yes
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Source:
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Moraxella sp. Hmsc061h09. Organism_taxid: 1715217. Gene: hmpref2573_04170. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.50Å
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R-factor:
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0.133
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R-free:
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0.153
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Authors:
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P.J.Stogios,E.Evdokimova,Z.Wawrzak,A.Savchenko,W.F.Anderson, K.J.Satchell,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid)
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Key ref:
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P.J.Stogios
et al.
(2018).
Substrate Recognition by a Colistin Resistance Enzyme from Moraxella catarrhalis.
ACS Chem Biol,
13,
1322-1332.
PubMed id:
DOI:
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Date:
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16-Nov-17
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Release date:
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31-Jan-18
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PROCHECK
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Headers
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References
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A0A1E9VP98
(A0A1E9VP98_9GAMM) -
Phosphoethanolamine transferase from Moraxella sp. HMSC061H09
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Seq:
Struc:
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578 a.a.
335 a.a.*
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Key: |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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ACS Chem Biol
13:1322-1332
(2018)
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PubMed id:
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Substrate Recognition by a Colistin Resistance Enzyme from Moraxella catarrhalis.
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P.J.Stogios,
G.Cox,
H.L.Zubyk,
E.Evdokimova,
Z.Wawrzak,
G.D.Wright,
A.Savchenko.
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ABSTRACT
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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.
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