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The Bacillus licheniformis BlaP β‐lactamase as a model protein scaffold to study the insertion of protein fragments
Author(s) -
Vandevenne Marylène,
Filee Patrice,
Scarafone Natacha,
Cloes Benoît,
Gaspard Gilles,
Yilmaz Nursel,
Dumoulin Mireille,
François JeanMarie,
Frère JeanMarie,
Galleni Moreno
Publication year - 2007
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.072912407
Subject(s) - bacillus licheniformis , heterologous , protein engineering , chitin , chemistry , fusion protein , scaffold protein , protein domain , protein structure , biochemistry , biology , recombinant dna , enzyme , genetics , bacteria , gene , bacillus subtilis , chitosan , signal transduction
Abstract 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 β‐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 β‐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.