1bh6
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structure of subtilisin DY inhibited by | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Eschenburg, S.]] | [[Category: Eschenburg, S.]] | ||
[[Category: Genov, N.]] | [[Category: Genov, N.]] | ||
| - | [[Category: Wilson, K | + | [[Category: Wilson, K S.]] |
[[Category: 1BH]] | [[Category: 1BH]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: subtilisin]] | [[Category: subtilisin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:14 2008'' |
Revision as of 09:55, 21 February 2008
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SUBTILISIN DY IN COMPLEX WITH THE SYNTHETIC INHIBITOR N-BENZYLOXYCARBONYL-ALA-PRO-PHE-CHLOROMETHYL KETONE
Overview
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.
About this Structure
1BH6 is a Single protein structure of sequence from Bacillus licheniformis with , and as ligands. Active as Subtilisin, with EC number 3.4.21.62 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg., Eschenburg S, Genov N, Peters K, Fittkau S, Stoeva S, Wilson KS, Betzel C, Eur J Biochem. 1998 Oct 15;257(2):309-18. PMID:9826175
Page seeded by OCA on Thu Feb 21 11:55:14 2008
Categories: Bacillus licheniformis | Single protein | Subtilisin | Betzel, C. | Eschenburg, S. | Genov, N. | Wilson, K S. | 1BH | CA | NA | Hydrolase | Protein degradation
