Título:
|
Crystallization and preliminary X-ray diffraction analysis of the N-terminal domain of Paenibacillus barcinonensis xylanase 10C containing the CBM22-1-CBM22-2 tandem
|
Autor/a:
|
Sainz Polo, M. A.; González Navarro, Beatriz; Pastor Blasco, Francisco I. Javier; Sanz Aparicio, J.
|
Otros autores:
|
Universitat de Barcelona |
Abstract:
|
A construct containing the CBM22-1-CBM22-2 tandem forming the N-terminal domain of Paenibacillus barcinonensis xylanase 10C (Xyn10C) has been purified and crystallized. A xylan-binding function and an affinity for mixed [beta]-1,3/[beta]-1,4 glucans have previously been demonstrated for some members of the CBM22 family. The sequence of the tandem is homologous to the N-terminal domains found in several thermophilic enzymes. Crystals of this tandem were grown by the streak-seeding method after a long optimization strategy. The structure has been determined by molecular replacement to a resolution of 2.43 Å and refinement is under way. This study represents the first structure containing two contiguous CBM22 modules, which will contribute to a better understanding of the role that this multiplicity plays in fine-tuning substrate affinity |
Materia(s):
|
-Enzims microbians -Biopolímers -Biotecnologia -Microbial enzymes -Biopolymers -Biotechnology |
Derechos:
|
(c) International Union of Crystallography, 2015
|
Tipo de documento:
|
Artículo Artículo - Versión publicada |
Editor:
|
International Union of Crystallography
|
Compartir:
|
|