1sca
From Proteopedia
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'''ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT''' | '''ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT''' | ||
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[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
[[Category: Steinmetz, A C.U.]] | [[Category: Steinmetz, A C.U.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:32:23 2008'' | |
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Revision as of 05:32, 3 May 2008
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. 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 Sat May 3 08:32:23 2008
