5MX9

High resolution crystal structure of the MCR-2 catalytic domain


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.12 Å
  • R-Value Free: 0.145 
  • R-Value Work: 0.133 
  • R-Value Observed: 0.134 

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This is version 1.2 of the entry. See complete history


Literature

1.12 angstrom resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2.

Coates, K.Walsh, T.R.Spencer, J.Hinchliffe, P.

(2017) Acta Crystallogr F Struct Biol Commun 73: 443-449

  • DOI: https://doi.org/10.1107/S2053230X17009669
  • Primary Citation of Related Structures:  
    5MX9

  • PubMed Abstract: 

    MCR-2 confers resistance to colistin, a `last-line' antibiotic against extensively resistant Gram-negative pathogens. It is a plasmid-encoded phosphoethanolamine transferase that is closely related to MCR-1. To understand the diversity in the MCR family, the 1.12 Å resolution crystal structure of the catalytic domain of MCR-2 was determined. Variable amino acids are located distant from both the di-zinc active site and the membrane-proximal face. The exceptionally high resolution will provide an accurate starting model for further mechanistic studies.


  • Organizational Affiliation

    School of Cellular and Molecular Medicine, University of Bristol, Bristol BS8 1TD, England.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Phosphatidylethanolamine transferase Mcr-2324Escherichia coliMutation(s): 0 
Gene Names: mcr-2
UniProt
Find proteins for A0A1C3NEV1 (Escherichia coli)
Explore A0A1C3NEV1 
Go to UniProtKB:  A0A1C3NEV1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A1C3NEV1
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.12 Å
  • R-Value Free: 0.145 
  • R-Value Work: 0.133 
  • R-Value Observed: 0.134 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 44.818α = 90
b = 53.31β = 90
c = 117.509γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
DIALSdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Medical Research Council (United Kingdom)United KingdomMR/P007295/1

Revision History  (Full details and data files)

  • Version 1.0: 2017-08-09
    Type: Initial release
  • Version 1.1: 2017-08-23
    Changes: Database references
  • Version 1.2: 2024-01-17
    Changes: Data collection, Database references, Derived calculations, Refinement description