Reference : The Bacillus licheniformis BlaP beta-lactamase as a model protein scaffold to study the ...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/76059
The Bacillus licheniformis BlaP beta-lactamase as a model protein scaffold to study the insertion of protein fragments.
English
Vandevenne, Marylène [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Filée, Patrice [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Scarafone, Natacha mailto [Université de Liège - ULg > Département des sciences de la vie > Enzymologie et repliement des protéines >]
Cloes, Benoit [> > > >]
Gaspard, Gilles [> > > >]
Yilmaz, Nursel [> > > >]
Dumoulin, Mireille mailto [Université de Liège - ULg > Département des sciences de la vie > Enzymologie et repliement des protéines >]
François, Jean-Marie mailto [Université de Liège - ULg > Département des sciences de la vie > Macromolécules biologiques >]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Galleni, Moreno mailto [Université de Liège - ULg > Département des sciences de la vie > Macromolécules biologiques >]
2007
Protein Science : A Publication of the Protein Society
Cold Spring Harbor Laboratory Press
16
10
2260-71
Yes (verified by ORBi)
International
0961-8368
1469-896X
Woodbury
NY
[en] Bacillus/enzymology ; Bacterial Proteins/chemistry/genetics ; Chitin/metabolism ; Enzyme Stability ; Hexosaminidases/chemistry ; Models, Molecular ; Protein Denaturation ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry ; beta-Lactamases/chemistry/genetics
[en] Using genetic engineering technologies, the chitin-binding domain (ChBD) of the human macrophage chitotriosidase has been inserted into the host protein BlaP, a class A beta-lactamase produced by Bacillus licheniformis. The product of this construction behaved as a soluble chimeric protein that conserves both the capacity to bind chitin and to hydrolyze beta-lactam moiety. Here we describe the biochemical and biophysical properties of this protein (BlaPChBD). This work contributes to a better understanding of the reciprocal structural and functional effects of the insertion on the host protein scaffold and the heterologous structured protein fragments. The use of BlaP as a protein carrier represents an efficient approach to the functional study of heterologous protein fragments.
http://hdl.handle.net/2268/76059
also: http://hdl.handle.net/2268/78220
10.1110/ps.072912407

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