Reference : Crystal structure of a cold-adapted class C beta-lactamase.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/15205
Crystal structure of a cold-adapted class C beta-lactamase.
English
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 [> > > >]
2008
FEBS Journal
Blackwell Publishing
275
8
1687-97
Yes (verified by ORBi)
International
1742-464X
Oxford
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.
http://hdl.handle.net/2268/15205
10.1111/j.1742-4658.2008.06324.x

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