Crystal structure of the alkaline proteinase Savinase™ from Bacillus lentus at 1.4 Å resolution
Identifieur interne : 003252 ( Main/Exploration ); précédent : 003251; suivant : 003253Crystal structure of the alkaline proteinase Savinase™ from Bacillus lentus at 1.4 Å resolution
Auteurs : Christian Betzel [Allemagne] ; Silke Klupsch [Allemagne] ; Gerlind Papendorf [Allemagne] ; Sven Hastrup [Danemark] ; Sven Branner [Danemark] ; Keith S. Wilson [Allemagne]Source :
- Journal of Molecular Biology [ 0022-2836 ] ; 1991.
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 Å resolution. The starting model was that of subtilisin Carlsberg. A comparison to the structures of the closely related subtilising 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 hydrophic 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 (= (Σ∥Fo¦− ¦Fc∥) (Σ¦Fo¦)) is 17.3% at 1.4 A ̊ resolution.
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DOI: 10.1016/0022-2836(92)90662-4
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Wilson</name><affiliation wicri:level="1"><country xml:lang="fr">Allemagne</country><wicri:regionArea>European Molecular Biology Laboratory (EMBL), c/o DESY, Notkestrasse 85, D-2000 Hamburg 52</wicri:regionArea><wicri:noRegion>D-2000 Hamburg 52</wicri:noRegion><wicri:noRegion>D-2000 Hamburg 52</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Molecular Biology</title><title level="j" type="abbrev">YJMBI</title><idno type="ISSN">0022-2836</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1991">1991</date><biblScope unit="volume">223</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="427">427</biblScope><biblScope unit="page" to="445">445</biblScope></imprint><idno type="ISSN">0022-2836</idno></series><idno type="istex">72874AB819315FE49D7E72F4FFF0F74225E36E3C</idno><idno type="DOI">10.1016/0022-2836(92)90662-4</idno><idno type="PII">0022-2836(92)90662-4</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0022-2836</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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 Å resolution. The starting model was that of subtilisin Carlsberg. A comparison to the structures of the closely related subtilising 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 hydrophic 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 (= (Σ∥Fo¦− ¦Fc∥) (Σ¦Fo¦)) is 17.3% at 1.4 A ̊ resolution.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>Danemark</li></country></list><tree><country name="Allemagne"><noRegion><name sortKey="Betzel, Christian" sort="Betzel, Christian" uniqKey="Betzel C" first="Christian" last="Betzel">Christian Betzel</name></noRegion><name sortKey="Klupsch, Silke" sort="Klupsch, Silke" uniqKey="Klupsch S" first="Silke" last="Klupsch">Silke Klupsch</name><name sortKey="Papendorf, Gerlind" sort="Papendorf, Gerlind" uniqKey="Papendorf G" first="Gerlind" last="Papendorf">Gerlind Papendorf</name><name sortKey="Wilson, Keith S" sort="Wilson, Keith S" uniqKey="Wilson K" first="Keith S." last="Wilson">Keith S. Wilson</name></country><country name="Danemark"><noRegion><name sortKey="Hastrup, Sven" sort="Hastrup, Sven" uniqKey="Hastrup S" first="Sven" last="Hastrup">Sven Hastrup</name></noRegion><name sortKey="Branner, Sven" sort="Branner, Sven" uniqKey="Branner S" first="Sven" last="Branner">Sven Branner</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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