1SVN

SAVINASE

1SVN の概要

• エントリーDOI: 10.2210/pdb1svn/pdb
• 分子名称: SAVINASE (TM), CALCIUM ION (3 entities in total)
• 機能のキーワード: hydrolase, sporulation, serine protease, calcium-binding
• 由来する生物種: Bacillus lentus
• 細胞内の位置: Secreted: P29600
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26798.54

構造登録者

Betzel, C.,Klupsch, S.,Papendorf, G.,Hastrup, S.,Branner, S.,Wilson, K.S. (登録日: 1995-09-01, 公開日: 1996-10-14, 最終更新日: 2024-03-06)

主引用文献

Betzel, C.,Klupsch, S.,Papendorf, G.,Hastrup, S.,Branner, S.,Wilson, K.S.
Crystal structure of the alkaline proteinase Savinase from Bacillus lentus at 1.4 A resolution.
J.Mol.Biol., 223:427-445, 1992

PubMed Abstract: 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].

PubMed: 1738156
DOI: 10.1016/0022-2836(92)90662-4

実験手法

X-RAY DIFFRACTION (1.4 Å)