1BFK

CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG IN 40% ACETONITRILE

Summary for 1BFK

• Entry DOI: 10.2210/pdb1bfk/pdb
• Descriptor: SUBTILISIN CARLSBERG, CALCIUM ION, ACETONITRILE, ... (4 entities in total)
• Functional Keywords: serine protease, organic solvent, mixtures
• Biological source: Bacillus licheniformis
• Cellular location: Secreted: P00780
• Total number of polymer chains: 1
• Total formula weight: 27551.54

Authors

Schmitke, J.L.,Stern, L.J.,Klibanov, A.M. (deposition date: 1998-05-21, release date: 1998-10-28, Last modification date: 2024-05-22)

Primary citation

Schmitke, J.L.,Stern, L.J.,Klibanov, A.M.
Organic solvent binding to crystalline subtilisin1 in mostly aqueous media and in the neat solvents.
Biochem.Biophys.Res.Commun., 248:273-277, 1998

PubMed Abstract: The X-ray crystal structures of the protease subtilisin Carlsberg in 40% acetonitrile and in 20% dioxane have been determined to at least 2.3 A resolution, and their solvent binding patterns have been compared to those observed in the neat organic solvents. The structures of the protein in the two aqueous-organic mixtures are essentially the same as in pure water, acetonitrile, and dioxane. Interestingly, the enzyme-bound organic solvent molecules tend to congregate in the active site. Three of the five bound acetonitrile molecules observed in the structure of subtilisin in 40% acetonitrile are situated in the enzyme active site, as is the single enzyme-bound dioxane molecule observed in 20% dioxane (whose location is distinct from that of any bound acetonitrile molecule). Furthermore, the organic solvent molecules detected in the enzyme active site in the aqueous-organic mixtures are in the same locations as in the structures in the corresponding neat organic solvents.

PubMed: 9675126
DOI: 10.1006/bbrc.1998.8937

Experimental method

X-RAY DIFFRACTION (2.3 Å)