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[[Image:1sub.jpg|left|200px]]
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{{STRUCTURE_1sub|  PDB=1sub  |  SCENE=  }}
'''CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN'''


==CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN==
<StructureSection load='1sub' size='340' side='right'caption='[[1sub]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1sub]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SUB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=1sub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sub OCA], [https://pdbe.org/1sub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sub RCSB], [https://www.ebi.ac.uk/pdbsum/1sub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sub ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SUBT_BACAM SUBT_BACAM] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.<ref>PMID:12524032</ref>
== 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/su/1sub_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1sub ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A version of subtilisin BPN' lacking the high affinity calcium site (site A) has been produced through genetic engineering methods, and its crystal structure refined at 1.8 A resolution. This protein and the corresponding version containing the calcium A site are described and compared. The deletion of residues 75-83 was made in the context of four site-specific replacements previously shown to stabilize subtilisin. The helix that in wild type is interrupted by the calcium binding loop, is continuous in the deletion mutant, with normal geometry. A few residues adjacent to the loop, principally those that were involved in calcium coordination, are repositioned and/or destabilized by the deletion. Because refolding is greatly facilitated by the absence of the Ca-loop, this protein offers a new vehicle for analysis and dissection of the folding reaction. This is among the largest internal changes to a protein to be described at atomic resolution.


==Overview==
Calcium-independent subtilisin by design.,Gallagher T, Bryan P, Gilliland GL Proteins. 1993 Jun;16(2):205-13. PMID:8332608<ref>PMID:8332608</ref>
A version of subtilisin BPN' lacking the high affinity calcium site (site A) has been produced through genetic engineering methods, and its crystal structure refined at 1.8 A resolution. This protein and the corresponding version containing the calcium A site are described and compared. The deletion of residues 75-83 was made in the context of four site-specific replacements previously shown to stabilize subtilisin. The helix that in wild type is interrupted by the calcium binding loop, is continuous in the deletion mutant, with normal geometry. A few residues adjacent to the loop, principally those that were involved in calcium coordination, are repositioned and/or destabilized by the deletion. Because refolding is greatly facilitated by the absence of the Ca-loop, this protein offers a new vehicle for analysis and dissection of the folding reaction. This is among the largest internal changes to a protein to be described at atomic resolution.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1SUB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUB OCA].
</div>
<div class="pdbe-citations 1sub" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Calcium-independent subtilisin by design., Gallagher T, Bryan P, Gilliland GL, Proteins. 1993 Jun;16(2):205-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8332608 8332608]
*[[Subtilisin 3D structures|Subtilisin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus amyloliquefaciens]]
[[Category: Bacillus amyloliquefaciens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Subtilisin]]
[[Category: Bryan P]]
[[Category: Bryan, P.]]
[[Category: Gallagher T]]
[[Category: Gallagher, T.]]
[[Category: Gilliland GL]]
[[Category: Gilliland, G L.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:08:39 2008''

Latest revision as of 07:27, 9 October 2024

CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN

1sub, resolution 1.75Å

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