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PDBsum entry 1svn
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Serine protease
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PDB id
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1svn
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the alkaline proteinase savinase from bacillus lentus at 1.4 a resolution.
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Authors
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C.Betzel,
S.Klupsch,
G.Papendorf,
S.Hastrup,
S.Branner,
K.S.Wilson.
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Ref.
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J Mol Biol, 1992,
223,
427-445.
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PubMed id
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Abstract
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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].
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Secondary reference #1
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Title
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Crystallization and preliminary X-Ray diffraction studies of an alkaline protease from bacillus lentus.
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Authors
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C.Betzel,
Z.Dauter,
M.Dauter,
M.Ingelman,
G.Papendorf,
K.S.Wilson,
S.Branner.
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Ref.
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J Mol Biol, 1988,
204,
803-804.
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PubMed id
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