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2015-02

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Si us plau utilitzeu sempre aquest identificador per citar o enllaçar aquest document: https://hdl.handle.net/2445/62364

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

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Recurs relacionat

http://dx.doi.org/10.1107/S2053230X14027496

Resum

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

Matèries

Enzims microbians, Biopolímers, Biotecnologia

Matèries (anglès)

Microbial enzymes, Biopolymers, Biotechnology

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Articles publicats en revistes (Genètica, Microbiologia i Estadística)

Citació

SAINZ POLO, M. A., et al. Crystallization and preliminary X-ray diffraction analysis of the N-terminal domain of Paenibacillus barcinonensis xylanase 10C containing the CBM22-1-CBM22-2 tandem. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2015. Vol. 71, num. 2, pags. 136-140. ISSN 1744-3091. [consulted: 14 of August of 2026]. Available at: https://hdl.handle.net/2445/62364

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