Structure determination and analysis of a bacterial chymotrypsin from Cellulomonas bogoriensis

The crystal structure of a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis has been determined using data to 1.78 Å resolution and refined to a crystallographic R factor of 0.167. The crystal structure reveals a large P1 substrate‐specificity pocket, as expected for chymotrypsins...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2007-04, Vol.63 (4), p.266-269
Main Authors: Bott, R., Saldajeno, M. L., Shaw, A., Kolkman, M. A. B., Jones, B. E.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacteria
Bacterial Proteins - chemistry
Cellulomonas
Cellulomonas - chemistry
Cellulomonas bogoriensis
chymotrypsin
Chymotrypsin - chemistry
Crystallization
Hydrogen Bonding
Molecular Sequence Data
Protein Conformation
Protein Folding
Protein Structure Communications
Sequence Homology, Amino Acid
Substrate Specificity
X-Ray Diffraction
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Summary:The crystal structure of a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis has been determined using data to 1.78 Å resolution and refined to a crystallographic R factor of 0.167. The crystal structure reveals a large P1 substrate‐specificity pocket, as expected for chymotrypsins. The structure is compared with close structural homologues. This comparison does not reveal clear reasons for the alkali tolerance of the enzyme, but the greater compactness of the structure and lowered hydrogen bonding may play a role.
ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309107008937