2ea3
From Proteopedia
Crystal Structure Of Cellulomonas Bogoriensis Chymotrypsin
Overview
The crystal structure of a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis has been determined using data to 1.78 A 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.
About this Structure
Full crystallographic information is available from OCA.
Reference
Structure determination and analysis of a bacterial chymotrypsin from Cellulomonas bogoriensis., Shaw A, Saldajeno ML, Kolkman MA, Jones BE, Bott R, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):266-9. Epub 2007 Mar 23. PMID:17401191 Page seeded by OCA on Sun May 4 02:13:35 2008
