PDBsum entry 2qz6

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protein links
Hydrolase PDB id
Protein chain
349 a.a. *
Waters ×134
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: First crystal structure of a psychrophile class c beta- lactamase
Structure: Beta-lactamase. Chain: a. Synonym: cephalosporinase. Ec:
Source: Pseudomonas fluorescens. Organism_taxid: 294. Strain: tae 4
2.26Å     R-factor:   0.192     R-free:   0.243
Authors: C.Michaux,J.Massant,F.Kerff,P.Charlier,J.Wouters
Key ref: C.Michaux et al. (2008). Crystal structure of a cold-adapted class C beta-lactamase. FEBS J, 275, 1687-1697. PubMed id: 18312599
16-Aug-07     Release date:   18-Mar-08    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P85302  (AMPC_PSEFL) -  Beta-lactamase
358 a.a.
349 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Beta-lactamase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Penicillin Biosynthesis and Metabolism
      Reaction: A beta-lactam + H2O = a substituted beta-amino acid
      Cofactor: Zn(2+)
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     periplasmic space   2 terms 
  Biological process     response to antibiotic   2 terms 
  Biochemical function     hydrolase activity     2 terms  


FEBS J 275:1687-1697 (2008)
PubMed id: 18312599  
Crystal structure of a cold-adapted class C beta-lactamase.
C.Michaux, J.Massant, F.Kerff, J.M.Frère, J.D.Docquier, I.Vandenberghe, B.Samyn, A.Pierrard, G.Feller, P.Charlier, J.Van Beeumen, J.Wouters.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20646925 A.Casanueva, M.Tuffin, C.Cary, and D.A.Cowan (2010).
Molecular adaptations to psychrophily: the impact of 'omic' technologies.
  Trends Microbiol, 18, 374-381.  
19901091 D.Girlich, L.Poirel, and P.Nordmann (2010).
Novel ambler class A carbapenem-hydrolyzing beta-lactamase from a Pseudomonas fluorescens isolate from the Seine River, Paris, France.
  Antimicrob Agents Chemother, 54, 328-332.  
20000704 M.Toth, C.Smith, H.Frase, S.Mobashery, and S.Vakulenko (2010).
An antibiotic-resistance enzyme from a deep-sea bacterium.
  J Am Chem Soc, 132, 816-823.
PDB code: 3lez
19136439 G.A.Jacoby (2009).
AmpC beta-lactamases.
  Clin Microbiol Rev, 22, 161.  
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