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1be6
From Proteopedia
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TRANS-CINNAMOYL-SUBTILISIN IN ANHYDROUS ACETONITRILE
Overview
The x-ray crystal structures of trans-cinnamoyl-subtilisin, an acyl-enzyme, covalent intermediate of the serine protease subtilisin Carlsberg, have, been determined to 2.2-A resolution in anhydrous acetonitrile and in, water. The cinnamoyl-subtilisin structures are virtually identical in the, two solvents. In addition, their enzyme portions are nearly, indistinguishable from previously determined structures of the free enzyme, in acetonitrile and in water; thus, acylation in either aqueous or, nonaqueous solvent causes no appreciable conformational changes. However, the locations of bound solvent molecules in the active site of the acyl-, and free enzyme forms in acetonitrile and in water are distinct. Such, differences in the active site solvation may contribute to the observed, ... [(full description)]
About this Structure
1BE6 is a [Single protein] structure of sequence from [Bacillus licheniformis] with CA, TCA and CCN as [ligands]. Active as [[1]], with EC number [3.4.21.62]. Full crystallographic information is available from [OCA].
Reference
Comparison of x-ray crystal structures of an acyl-enzyme intermediate of subtilisin Carlsberg formed in anhydrous acetonitrile and in water., Schmitke JL, Stern LJ, Klibanov AM, Proc Natl Acad Sci U S A. 1998 Oct 27;95(22):12918-23. PMID:9789015
Page seeded by OCA on Mon Oct 29 20:58:03 2007
