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. 1993 Sep 15;90(18):8653–8657. doi: 10.1073/pnas.90.18.8653

Enzyme crystal structure in a neat organic solvent.

P A Fitzpatrick 1, A C Steinmetz 1, D Ringe 1, A M Klibanov 1
PMCID: PMC47416  PMID: 8378343

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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