1sca
From Proteopedia
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ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT
Overview
The crystal structure of the serine protease subtilisin Carlsberg in, anhydrous acetonitrile was determined at 2.3 A resolution. It was found to, be essentially identical to the three-dimensional structure of the enzyme, in water; the differences observed were smaller than those between two, independently determined structures in aqueous solution. The hydrogen bond, system of the catalytic triad is intact in acetonitrile. The majority (99, of 119) of enzyme-bound, structural water molecules have such a great, affinity to subtilisin that they are not displaced even in anhydrous, acetonitrile. Of the 12 enzyme-bound acetonitrile molecules, 4 displace, water molecules and 8 bind where no water had been observed before., One-third of all subtilisin-bound acetonitrile molecules reside in the, active center, occupying the same region (P1, P2, and P3 binding sites) as, the specific protein inhibitor eglin c.
About this Structure
1SCA is a Single protein structure of sequence from Bacillus licheniformis with CA and NA as ligands. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.
Reference
Enzyme crystal structure in a neat organic solvent., Fitzpatrick PA, Steinmetz AC, Ringe D, Klibanov AM, Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8653-7. PMID:8378343
Page seeded by OCA on Wed Nov 21 02:16:09 2007
