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[[Image:1dbi.gif|left|200px]]
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{{STRUCTURE_1dbi|  PDB=1dbi  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE PROTEASE'''


==CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE PROTEASE==
<StructureSection load='1dbi' size='340' side='right'caption='[[1dbi]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dbi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._Ak1 Bacillus sp. Ak1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DBI 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1dbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dbi OCA], [https://pdbe.org/1dbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dbi RCSB], [https://www.ebi.ac.uk/pdbsum/1dbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dbi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/THES_BACSJ THES_BACSJ]
== 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/db/1dbi_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=1dbi ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Proteins of the subtilisin superfamily (subtilases) are widely distributed through many living species, where they perform a variety of processing functions. They are also used extensively in industry. In many of these enzymes, bound calcium ions play a key role in protecting against autolysis and thermal denaturation. We have determined the crystal structure of a highly thermostable protease from Bacillus sp. Ak.1 that is strongly stabilized by calcium. The crystal structure, determined at 1.8 A resolution (R=0. 182, Rfree=0.247), reveals the presence of four bound cations, three Ca(2+) and one Na(+). Two of the Ca(2+) binding sites, Ca-1 and Ca-2, correspond to sites also found in thermitase and the mesophilic subtilisins. The third calcium ion, however, is at a novel site that is created by two key amino acid substitutions near Ca-1, and has not been observed in any other subtilase. This site, acting cooperatively with Ca-1, appears to give substantially enhanced thermostability, compared with thermitase. Comparisons with the mesophilic subtilisins also point to the importance of aromatic clusters, reduced hydrophobic surface and constrained N and C termini in enhancing the thermostability of thermitase and Ak.1 protease. The Ak.1 protease also contains an unusual Cys-X-Cys disulfide bridge that modifies the active site cleft geometry.


==Overview==
Calcium-mediated thermostability in the subtilisin superfamily: the crystal structure of Bacillus Ak.1 protease at 1.8 A resolution.,Smith CA, Toogood HS, Baker HM, Daniel RM, Baker EN J Mol Biol. 1999 Dec 10;294(4):1027-40. PMID:10588904<ref>PMID:10588904</ref>
Proteins of the subtilisin superfamily (subtilases) are widely distributed through many living species, where they perform a variety of processing functions. They are also used extensively in industry. In many of these enzymes, bound calcium ions play a key role in protecting against autolysis and thermal denaturation. We have determined the crystal structure of a highly thermostable protease from Bacillus sp. Ak.1 that is strongly stabilized by calcium. The crystal structure, determined at 1.8 A resolution (R=0. 182, Rfree=0.247), reveals the presence of four bound cations, three Ca(2+) and one Na(+). Two of the Ca(2+) binding sites, Ca-1 and Ca-2, correspond to sites also found in thermitase and the mesophilic subtilisins. The third calcium ion, however, is at a novel site that is created by two key amino acid substitutions near Ca-1, and has not been observed in any other subtilase. This site, acting cooperatively with Ca-1, appears to give substantially enhanced thermostability, compared with thermitase. Comparisons with the mesophilic subtilisins also point to the importance of aromatic clusters, reduced hydrophobic surface and constrained N and C termini in enhancing the thermostability of thermitase and Ak.1 protease. The Ak.1 protease also contains an unusual Cys-X-Cys disulfide bridge that modifies the active site cleft geometry.


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


==Reference==
==See Also==
Calcium-mediated thermostability in the subtilisin superfamily: the crystal structure of Bacillus Ak.1 protease at 1.8 A resolution., Smith CA, Toogood HS, Baker HM, Daniel RM, Baker EN, J Mol Biol. 1999 Dec 10;294(4):1027-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10588904 10588904]
*[[Proteinase 3D structures|Proteinase 3D structures]]
[[Category: Bacillus sp.]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Baker, E N.]]
__TOC__
[[Category: Baker, H M.]]
</StructureSection>
[[Category: Daniel, R M.]]
[[Category: Bacillus sp. Ak1]]
[[Category: Smith, C A.]]
[[Category: Large Structures]]
[[Category: Toogood, H S.]]
[[Category: Baker EN]]
[[Category: Hydrolase]]
[[Category: Baker HM]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:39:33 2008''
[[Category: Daniel RM]]
[[Category: Smith CA]]
[[Category: Toogood HS]]
Retrieved from "https://proteopedia.org/1dbi"