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

Catherine Michaux, Jan Massant, Frédéric Kerff, Jean Marie Frère, Jean Denis Docquier, Isabel Vandenberghe, Bart Samyn, Annick Pierrard, Georges Feller, Paulette Charlier, Jozef Van Beeumen, Johan Wouters

Research output: Contribution to journalArticlepeer-review


In this study, the crystal structure of a class C β-lactamase from a psychrophilic organism, Pseudomonas fluorescens, has been refined to 2.2 Å 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 β-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.

Original languageEnglish
Pages (from-to)1687-1697
Number of pages11
JournalFEBS Journal
Issue number8
Publication statusPublished - 1 Apr 2008


  • Class C β-lactamase
  • Cold adaptation
  • Psychrophile
  • Weak interactions
  • X-ray structure


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