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1bh6

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==Overview==
==Overview==
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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.
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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.]]
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[[Category: Wilson, K.S.]]
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[[Category: Wilson, K S.]]
[[Category: 1BH]]
[[Category: 1BH]]
[[Category: CA]]
[[Category: CA]]
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[[Category: subtilisin]]
[[Category: subtilisin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:32:54 2008''
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''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

Image:1bh6.gif

1bh6, resolution 1.75Å

Drag the structure with the mouse to rotate

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

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