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CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG IN 40% ACETONITRILE
Structural highlights
FunctionSUBC_BACLI Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (Ref.4, PubMed:11109488). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488).[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Organic solvent binding to crystalline subtilisin1 in mostly aqueous media and in the neat solvents.,Schmitke JL, Stern LJ, Klibanov AM Biochem Biophys Res Commun. 1998 Jul 20;248(2):273-7. PMID:9675126[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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