2QZ6

First crystal structure of a psychrophile class C beta-lactamase


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.26 Å
  • R-Value Free: 0.243 
  • R-Value Work: 0.190 
  • R-Value Observed: 0.192 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal structure of a cold-adapted class C beta-lactamase

Michaux, C.Massant, J.Kerff, F.Docquier, J.D.Vandenberghe, I.Samyn, B.Pierrard, A.Feller, G.Charlier, P.Van Beeumen, J.Wouters, J.

(2008) FEBS J 275: 1687-1697

  • DOI: https://doi.org/10.1111/j.1742-4658.2008.06324.x
  • Primary Citation of Related Structures:  
    2QZ6

  • PubMed Abstract: 

    In this study, the crystal structure of a class C beta-lactamase from a psychrophilic organism, Pseudomonas fluorescens, has been refined to 2.2 A resolution. It is one of the few solved crystal structures of psychrophilic proteins. The structure was compared with those of homologous mesophilic enzymes and of another, modeled, psychrophilic protein. The elucidation of the 3D structure of this enzyme provides additional insights into the features involved in cold adaptation. Structure comparison of the psychrophilic and mesophilic beta-lactamases shows that electrostatics seems to play a major role in low-temperature adaptation, with a lower total number of ionic interactions for cold enzymes. The psychrophilic enzymes are also characterized by a decreased number of hydrogen bonds, a lower content of prolines, and a lower percentage of arginines in comparison with lysines. All these features make the structure more flexible so that the enzyme can behave as an efficient catalyst at low temperatures.


  • Organizational Affiliation

    Chimie Biologique Structurale Laboratory, CPTS group, FUNDP, 61 rue de Bruxelles, Namur, Belgium. catherine.michaux@fundp.ac.be


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-lactamase358Pseudomonas fluorescensMutation(s): 0 
EC: 3.5.2.6
UniProt
Find proteins for P85302 (Pseudomonas fluorescens)
Explore P85302 
Go to UniProtKB:  P85302
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP85302
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.26 Å
  • R-Value Free: 0.243 
  • R-Value Work: 0.190 
  • R-Value Observed: 0.192 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 43.6α = 90
b = 69.7β = 90.9
c = 53.9γ = 90
Software Package:
Software NamePurpose
REFMACrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-03-18
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-10-25
    Changes: Data collection, Database references, Refinement description