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1dbi

From Proteopedia

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[[Image:1dbi.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE PROTEASE==
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|PDB= 1dbi |SIZE=350|CAPTION= <scene name='initialview01'>1dbi</scene>, resolution 1.8&Aring;
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<StructureSection load='1dbi' size='340' side='right'caption='[[1dbi]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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<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>
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|ACTIVITY=
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</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>
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|GENE=
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dbi OCA], [http://www.ebi.ac.uk/pdbsum/1dbi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dbi RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/THES_BACSJ THES_BACSJ]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/db/1dbi_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE PROTEASE'''
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==See Also==
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*[[Proteinase 3D structures|Proteinase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Bacillus sp. Ak1]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Baker EN]]
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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].
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[[Category: Baker HM]]
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[[Category: Daniel RM]]
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==Reference==
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[[Category: Smith CA]]
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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]
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[[Category: Toogood HS]]
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[[Category: Bacillus sp.]]
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[[Category: Single protein]]
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[[Category: Baker, E N.]]
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[[Category: Baker, H M.]]
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[[Category: Daniel, R M.]]
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[[Category: Smith, C A.]]
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[[Category: Toogood, H S.]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:38:20 2008''
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Current revision

CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE PROTEASE

PDB ID 1dbi

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