1af4
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CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG IN ANHYDROUS DIOXANE
OverviewOverview
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.
About this StructureAbout this Structure
1AF4 is a Single protein structure of sequence from Bacillus licheniformis with CA and DIO as ligands. Active as Subtilisin, with EC number 3.4.21.62 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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