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[[Image:1svn.gif|left|200px]]


{{Structure
==SAVINASE==
|PDB= 1svn |SIZE=350|CAPTION= <scene name='initialview01'>1svn</scene>, resolution 1.4&Aring;
<StructureSection load='1svn' size='340' side='right'caption='[[1svn]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
<table><tr><td colspan='2'>[[1svn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lederbergia_lenta Lederbergia lenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SVN FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1svn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svn OCA], [https://pdbe.org/1svn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1svn RCSB], [https://www.ebi.ac.uk/pdbsum/1svn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1svn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SUBS_LEDLE SUBS_LEDLE] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sv/1svn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1svn ConSurf].
<div style="clear:both"></div>


'''SAVINASE'''
==See Also==
 
*[[Subtilisin 3D structures|Subtilisin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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].
[[Category: Large Structures]]
 
[[Category: Lederbergia lenta]]
==About this Structure==
[[Category: Betzel C]]
1SVN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_lentus Bacillus lentus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVN OCA].
[[Category: Branner S]]
 
[[Category: Hastrup S]]
==Reference==
[[Category: Klupsch S]]
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:[http://www.ncbi.nlm.nih.gov/pubmed/1738156 1738156]
[[Category: Papendorf G]]
[[Category: Bacillus lentus]]
[[Category: Wilson KS]]
[[Category: Single protein]]
[[Category: Subtilisin]]
[[Category: Betzel, C.]]
[[Category: Branner, S.]]
[[Category: Hastrup, S.]]
[[Category: Klupsch, S.]]
[[Category: Papendorf, G.]]
[[Category: Wilson, K S.]]
[[Category: CA]]
[[Category: calcium-binding]]
[[Category: hydrolase]]
[[Category: serine protease]]
[[Category: sporulation]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:10:14 2008''

Latest revision as of 15:13, 6 March 2024

SAVINASESAVINASE

Structural highlights

1svn is a 1 chain structure with sequence from Lederbergia lenta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SUBS_LEDLE Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1svn, resolution 1.40Å

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