1bh6: Difference between revisions
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==Overview== | ==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 .. | 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== | ||
1BH6 is a | 1BH6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] with CA, NA and 1BH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Structure known Active Site: ACT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BH6 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: subtilisin]] | [[Category: subtilisin]] | ||
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Revision as of 14:49, 5 November 2007
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SUBTILISIN DY IN COMPLEX WITH THE SYNTHETIC INHIBITOR N-BENZYLOXYCARBONYL-ALA-PRO-PHE-CHLOROMETHYL KETONE
OverviewOverview
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 StructureAbout this Structure
1BH6 is a Single protein structure of sequence from Bacillus licheniformis with CA, NA and 1BH as ligands. Active as Subtilisin, with EC number 3.4.21.62 Structure known Active Site: ACT. Full crystallographic information is available from OCA.
ReferenceReference
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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