2WUI

Crystal Structure of MexZ, a key repressor responsible for antibiotic resistance in Pseudomonas aeruginosa.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.277 
  • R-Value Work: 0.227 
  • R-Value Observed: 0.229 

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This is version 1.2 of the entry. See complete history


Literature

Crystal Structure of Mexz, a Key Repressor Responsible for Antibiotic Resistance in Pseudomonas Aeruginosa.

Alguel, Y.Lu, D.Quade, N.Sauter, S.Zhang, X.

(2010) J Struct Biol 172: 305

  • DOI: https://doi.org/10.1016/j.jsb.2010.07.012
  • Primary Citation of Related Structures:  
    2WUI

  • PubMed Abstract: 

    Pseudomonas aeruginosa is responsible for around 10% of all hospital-acquired infections and the single most important pathogen of cystic fibrosis lungs. P. aeruginosa has high intrinsic and acquired antibiotic resistance, due to the extrusion of antibiotics by multidrug efflux pumps. The gene regulator MexZ controls the expression of mexXY, the efflux pump responsible for resistance to many drugs that are used for treating CF patients. MexZ is shown to be the most frequently mutated gene in P. aeruginosa isolated from CF patient lungs, confirming its importance in multidrug resistance. Here we present the crystal structure of MexZ at 2.9Å. Combining the structural information with biochemical data on key mutants identified, we provide an explanation for the structural and functional consequences of these mutants. This work provides a framework for further characterisation of MexZ in order to fully understand its regulation and induction.


  • Organizational Affiliation

    Division of Molecular Biosciences and Centre for Structural Biology, Imperial College London, London SW7 2AZ, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TRANSCRIPTIONAL REGULATOR210Pseudomonas aeruginosaMutation(s): 0 
UniProt
Find proteins for Q9RG61 (Pseudomonas aeruginosa)
Explore Q9RG61 
Go to UniProtKB:  Q9RG61
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9RG61
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.277 
  • R-Value Work: 0.227 
  • R-Value Observed: 0.229 
  • Space Group: H 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 177.055α = 90
b = 177.055β = 90
c = 54.658γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-08-18
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance