1af4: Difference between revisions

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{{STRUCTURE_1af4|  PDB=1af4  |  SCENE=  }}  
{{STRUCTURE_1af4|  PDB=1af4  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG IN ANHYDROUS DIOXANE'''
===CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG IN ANHYDROUS DIOXANE===




==Overview==
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The x-ray crystal structure of the serine protease subtilisin Carlsberg in anhydrous dioxane has been determined to 2.6-A resolution. The enzyme structure is found to be nearly indistinguishable from the structures previously determined in water and acetonitrile. Small changes in the side-chain conformations between the dioxane and water structures are of the same magnitude as those observed between two structures in different aqueous systems. Seven enzyme-bound dioxane molecules have been detected, each potentially forming at least one hydrogen bond with a subtilisin hydrogen-bond donor or bound water. Two of the bound dioxane molecules are in the active-site region, one in the P2 and another bridging the P1' and P3' pockets. The other five dioxane molecules are located on the surface of subtilisin at interprotein crystal contacts. The locations of the bound solvent in the dioxane structure are distinct from those in the structures in acetonitrile and in water.
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{{ABSTRACT_PUBMED_9113975}}


==About this Structure==
==About this Structure==
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[[Category: Organic solvent]]
[[Category: Organic solvent]]
[[Category: Serine protease]]
[[Category: Serine protease]]
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Revision as of 16:43, 30 June 2008

File:1af4.png

Template:STRUCTURE 1af4

CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG IN ANHYDROUS DIOXANECRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG IN ANHYDROUS DIOXANE

Template:ABSTRACT PUBMED 9113975

About this StructureAbout this Structure

1AF4 is a Single protein structure of sequence from Bacillus licheniformis. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of subtilisin Carlsberg in anhydrous dioxane and its comparison with those in water and acetonitrile., Schmitke JL, Stern LJ, Klibanov AM, Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4250-5. PMID:9113975

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