Structural highlights
Function
A2RQE2_9CELL
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shaw A, Saldajeno ML, Kolkman MA, Jones BE, Bott R. Structure determination and analysis of a bacterial chymotrypsin from Cellulomonas bogoriensis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):266-9. Epub 2007 Mar 23. PMID:17401191 doi:10.1107/S1744309107008937
