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Crystallization and preliminary X-ray diffraction analysis of the N-terminal domain of Paenibacillus barcinonensis xylanase 10C containing the CBM22-1-CBM22-2 tandem

AutorSainz-Polo, M. Ángela ; González, Beatriz ; Pastor, F.I.J.; Sanz-Aparicio, J.
Fecha de publicación2015
CitaciónActa Crystallographica Section F:Structural Biology Communications 71: 136- 140 (2015)
Resumen© 2015 International Union of Crystallography. 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 β-1,3/β-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 2.43Å 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.
Identificadoresdoi: 10.1107/S2053230X14027496
issn: 2053-230X
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