Download MendeleyCrystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg.
Eschenburg, S., Genov, N., Peters, K., Fittkau, S., Stoeva, S., Wilson, K.S., Betzel, C.(1998) Eur J Biochem 257: 309-318
- PubMed: 9826175
- DOI: https://doi.org/10.1046/j.1432-1327.1998.2570309.x
- Primary Citation of Related Structures:
1BH6 - PubMed Abstract:
The crystal structure of subtilisin DY inhibited by N-benzyloxycarbonyl-Ala-Pro-Phe-chloromethyl ketone has been solved by molecular replacement with subtilisin Carlsberg as the starting model. The model has been refined to a crystallographic R factor (= sigma absolute value [(absolute value Fo) - (absolute value Fc)] / sigma (absolute value of Fo) of 15.1% using X-ray diffraction data to 0.175 nm resolution. Subtilisin DY is an alkaline proteinase from the X-irradiated Japanese strain DY of Bacillus licheniformis, which normally produces subtilisin Carlsberg. It has very similar properties to subtilisin Carlsberg, with a slightly enhanced resistance to heat and guanidine hydrochloride-induced denaturation, in spite of the fact that the sequences of the two enzymes differ in 31 positions out of 274 residues. The close similarity in overall three-dimensional structure of subtilisins DY and Carlsberg and also their physicochemical properties, such as activity and stability, shows that nature aided by X-irradiation for rapid 'evolution' is able to accommodate considerable changes in sequence without substantial changes in property.
Organizational Affiliation:
European Molecular Biology Laboratory, Institute of Physiological Chemistry, Hamburg, Germany. Susanna@unisgi1.desy.de
