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PDBsum entry 2qz6

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protein links
Hydrolase PDB id
2qz6
Jmol
Contents
Protein chain
349 a.a. *
Waters ×134
* Residue conservation analysis
PDB id:
2qz6
Name: Hydrolase
Title: First crystal structure of a psychrophile class c beta- lactamase
Structure: Beta-lactamase. Chain: a. Synonym: cephalosporinase. Ec: 3.5.2.6
Source: Pseudomonas fluorescens. Organism_taxid: 294. Strain: tae 4
Resolution:
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
Date:
16-Aug-07     Release date:   18-Mar-08    
PROCHECK
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 Headers
 References

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

 Enzyme reactions 
   Enzyme class: E.C.3.5.2.6  - Beta-lactamase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
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.
 
  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.
 

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.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.