1svn
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SAVINASE
OverviewOverview
Savinase (EC3.4.21.14) is secreted by the alkalophilic bacterium Bacillus, lentus and is a representative of that subgroup of subtilisin enzymes with, maximum stability in the pH range 7 to 10 and high activity in the range 8, to 12. It is therefore of major industrial importance for use in, detergents. The crystal structure of the native form of Savinase has been, refined using X-ray diffraction data to 1.4 A resolution. The starting, model was that of subtilisin Carlsberg. A comparison to the structures of, the closely related subtilisins Carlsberg and BPN' and to the more distant, thermitase and proteinase K is presented. The structure of Savinase is, very similar to those of homologous Bacillus subtilisins. There are two, calcium ions in the structure, equivalent to the strong and the weak, calcium-binding sites in subtilisin Carlsberg and subtilisin BPN', well, known for their stabilizing effect on the subtilisins. The structure of, Savinase shows novel features that can be related to its stability and, activity. The relatively high number of salt bridges in Savinase is likely, to contribute to its high thermal stability. The non-conservative, substitutions and deletions in the hydrophobic binding pocket S1 result in, the most significant structural differences from the other subtilisins., The different composition of the S1 binding loop as well as the more, hydrophobic character of the substrate-binding region probably contribute, to the alkaline activity profile of the enzyme. The model of Savinase, contains 1880 protein atoms, 159 water molecules and two calcium ions. The, crystallographic R-factor [formula; see text].
About this StructureAbout this Structure
1SVN is a Single protein structure of sequence from Bacillus lentus with CA as ligand. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the alkaline proteinase Savinase from Bacillus lentus at 1.4 A resolution., Betzel C, Klupsch S, Papendorf G, Hastrup S, Branner S, Wilson KS, J Mol Biol. 1992 Jan 20;223(2):427-45. PMID:1738156
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