Reference : Crystal structure of a cold-adapted class C beta-lactamase.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Crystal structure of a cold-adapted class C beta-lactamase.
Michaux, Catherine [> > > >]
Massant, Jan [> > > >]
Kerff, Frédéric mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Docquier, Jean-Denis [> > > >]
Vandenberghe, Isabel [> > > >]
Samyn, Bart [> > > >]
Pierrard, Annick mailto [Université de Liège - ULg > Dép. d'électric., électron. et informat. (Inst.Montefiore) > Systèmes et modélisation >]
Feller, Georges mailto [Université de Liège - ULg > Département des sciences de la vie > Labo de biochimie >]
Charlier, Paulette mailto [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
Van Beeumen, Jozef [> > > >]
Wouters, Johan [> > > >]
FEBS Journal
Blackwell Publishing
Yes (verified by ORBi)
United Kingdom
[en] Amino Acid Sequence ; Cold Temperature ; Crystallography, X-Ray ; Enzyme Stability/drug effects ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Tertiary ; Pseudomonas fluorescens/enzymology ; Sequence Alignment ; Structural Homology, Protein ; Urea/pharmacology ; beta-Lactamases/chemistry/classification/metabolism
[en] 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.

File(s) associated to this reference

Fulltext file(s):

Restricted access
FebsJ_2008_Michaux.pdfPublisher postprint402.28 kBRequest copy

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.