Open AccessStructure determination and analysis of a bacterial chymotrypsin from Cellulomonas bogoriensis
Author(s) -
Bott R.,
Saldajeno M. L.,
Shaw A.,
Kolkman M. A. B.,
Jones B. E.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107008937
Subject(s) - crystal structure , chymotrypsin , hydrogen bond , crystallography , chemistry , substrate (aquarium) , hydrolase , materials science , enzyme , biochemistry , molecule , biology , trypsin , organic chemistry , ecology
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.