4YIN

Crystal structure of the extended-spectrum beta-lactamase OXA-145

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.248 
  • R-Value Work: 0.189 
  • R-Value Observed: 0.192 

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This is version 1.1 of the entry. See complete history. 


Literature

Structural insights into the loss of penicillinase and the gain of ceftazidimase activities by OXA-145 beta-lactamase in Pseudomonas aeruginosa.

Meziane-Cherif, D., Bonnet, R., Haouz, A., Courvalin, P.

(2016) J Antimicrob Chemother 71: 395-402

  • DOI: https://doi.org/10.1093/jac/dkv375
  • Primary Citation of Related Structures:  
    4YIN

  • PubMed Abstract: 

    We previously described extended-spectrum oxacillinase OXA-145 from Pseudomonas aeruginosa, which differs from narrow-spectrum OXA-35 by loss of Leu-155. The deletion results in loss of benzylpenicillin hydrolysis and acquisition of activity against ceftazidime. We report the crystal structure of OXA-145 and provide the basis of its switch in substrate specificity.

    • Organizational Affiliation: 

    Institut Pasteur, Unité des Agents Antibactériens, 25 rue du Docteur Roux, 75724 Paris cedex 15, France.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-lactamase
A, B
246Pseudomonas aeruginosaMutation(s): 0 
Gene Names: oxa145
EC: 3.5.2.6
UniProt
Find proteins for C0LZL5 (Pseudomonas aeruginosa)
Explore C0LZL5 
Go to UniProtKB:  C0LZL5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupC0LZL5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.248 
  • R-Value Work: 0.189 
  • R-Value Observed: 0.192 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 46.725α = 90
b = 91.182β = 90
c = 125.284γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
SCALAdata scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-02-10
    Type: Initial release
  • Version 1.1: 2018-04-18
    Changes: Data collection, Database references