1SCA

ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT

Summary for 1SCA

• Entry DOI: 10.2210/pdb1sca/pdb
• Descriptor: SUBTILISIN CARLSBERG, CALCIUM ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: serine protease
• Biological source: Bacillus licheniformis
• Cellular location: Secreted: P00780
• Total number of polymer chains: 1
• Total formula weight: 27409.35

Authors

Fitzpatrick, P.A.,Steinmetz, A.C.U.,Ringe, D.,Klibanov, A.M. (deposition date: 1993-07-19, release date: 1994-01-31, Last modification date: 2024-02-14)

Primary citation

Fitzpatrick, P.A.,Steinmetz, A.C.,Ringe, D.,Klibanov, A.M.
Enzyme crystal structure in a neat organic solvent.
Proc.Natl.Acad.Sci.USA, 90:8653-8657, 1993

PubMed 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.

PubMed: 8378343
DOI: 10.1073/pnas.90.18.8653

Experimental method

X-RAY DIFFRACTION (2 Å)