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Crystallization and preliminary X-ray analysis of the catalytic domains of Paenibacillus sp. strain FPU-7 cell-surface-expressed chitinase ChiW.

ABSTRACT: The polysaccharide chitin is effectively hydrolyzed and utilized as a carbon and nitrogen source by the Gram-positive bacterium Paenibacillus sp. strain FPU-7. ChiW is a unique cell-surface-expressed chitinase among the Paenibacillus sp. strain FPU-7-secreted chitinases. An N-terminally truncated ChiW protein, primarily comprised of the two catalytic domains of the full-length protein, was successfully overexpressed in Escherichia coli, purified as a functional recombinant protein with a molecular mass of approximately 98?kDa and crystallized. Preliminary X-ray analysis showed that the crystal diffracted to 1.93?Å resolution and belonged to the orthorhombic space group P212121, with unit-cell parameters a = 112.1, b = 128.2, c = 162.6?Å, suggesting the presence of two molecules in an asymmetric unit.

SUBMITTER: Itoh T 

PROVIDER: S-EPMC3944700 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of the catalytic domains of Paenibacillus sp. strain FPU-7 cell-surface-expressed chitinase ChiW.

Itoh Takafumi T   Hibi Takao T   Sugimoto Ikumi I   Suzuki Fumiko F   Fujii Yutaka Y   Taketo Akira A   Kimoto Hisashi H  

Acta crystallographica. Section F, Structural biology communications 20140219 Pt 3

The polysaccharide chitin is effectively hydrolyzed and utilized as a carbon and nitrogen source by the Gram-positive bacterium Paenibacillus sp. strain FPU-7. ChiW is a unique cell-surface-expressed chitinase among the Paenibacillus sp. strain FPU-7-secreted chitinases. An N-terminally truncated ChiW protein, primarily comprised of the two catalytic domains of the full-length protein, was successfully overexpressed in Escherichia coli, purified as a functional recombinant protein with a molecul  ...[more]