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1bfk

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[[Image:1bfk.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG IN 40% ACETONITRILE==
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|PDB= 1bfk |SIZE=350|CAPTION= <scene name='initialview01'>1bfk</scene>, resolution 2.3&Aring;
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<StructureSection load='1bfk' size='340' side='right'caption='[[1bfk]], [[Resolution|resolution]] 2.30&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> and <scene name='pdbligand=CCN:ACETONITRILE'>CCN</scene>
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<table><tr><td colspan='2'>[[1bfk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BFK FirstGlance]. <br>
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|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]
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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]] 2.3&#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=CCN:ACETONITRILE'>CCN</scene></td></tr>
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}}
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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=1bfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfk OCA], [https://pdbe.org/1bfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bfk RCSB], [https://www.ebi.ac.uk/pdbsum/1bfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bfk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SUBC_BACLI SUBC_BACLI] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (Ref.4, PubMed:11109488). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488).<ref>PMID:11109488</ref> <ref>PMID:4967581</ref>
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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/bf/1bfk_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=1bfk ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The X-ray crystal structures of the protease subtilisin Carlsberg in 40% acetonitrile and in 20% dioxane have been determined to at least 2.3 A resolution, and their solvent binding patterns have been compared to those observed in the neat organic solvents. The structures of the protein in the two aqueous-organic mixtures are essentially the same as in pure water, acetonitrile, and dioxane. Interestingly, the enzyme-bound organic solvent molecules tend to congregate in the active site. Three of the five bound acetonitrile molecules observed in the structure of subtilisin in 40% acetonitrile are situated in the enzyme active site, as is the single enzyme-bound dioxane molecule observed in 20% dioxane (whose location is distinct from that of any bound acetonitrile molecule). Furthermore, the organic solvent molecules detected in the enzyme active site in the aqueous-organic mixtures are in the same locations as in the structures in the corresponding neat organic solvents.
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'''CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG IN 40% ACETONITRILE'''
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Organic solvent binding to crystalline subtilisin1 in mostly aqueous media and in the neat solvents.,Schmitke JL, Stern LJ, Klibanov AM Biochem Biophys Res Commun. 1998 Jul 20;248(2):273-7. PMID:9675126<ref>PMID:9675126</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1bfk" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The X-ray crystal structures of the protease subtilisin Carlsberg in 40% acetonitrile and in 20% dioxane have been determined to at least 2.3 A resolution, and their solvent binding patterns have been compared to those observed in the neat organic solvents. The structures of the protein in the two aqueous-organic mixtures are essentially the same as in pure water, acetonitrile, and dioxane. Interestingly, the enzyme-bound organic solvent molecules tend to congregate in the active site. Three of the five bound acetonitrile molecules observed in the structure of subtilisin in 40% acetonitrile are situated in the enzyme active site, as is the single enzyme-bound dioxane molecule observed in 20% dioxane (whose location is distinct from that of any bound acetonitrile molecule). Furthermore, the organic solvent molecules detected in the enzyme active site in the aqueous-organic mixtures are in the same locations as in the structures in the corresponding neat organic solvents.
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*[[Subtilisin 3D structures|Subtilisin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1BFK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BFK OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Organic solvent binding to crystalline subtilisin1 in mostly aqueous media and in the neat solvents., Schmitke JL, Stern LJ, Klibanov AM, Biochem Biophys Res Commun. 1998 Jul 20;248(2):273-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9675126 9675126]
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[[Category: Bacillus licheniformis]]
[[Category: Bacillus licheniformis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Subtilisin]]
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[[Category: Klibanov AM]]
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[[Category: Klibanov, A M.]]
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[[Category: Schmitke JL]]
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[[Category: Schmitke, J L.]]
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[[Category: Stern LJ]]
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[[Category: Stern, L J.]]
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[[Category: CA]]
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[[Category: CCN]]
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[[Category: mixture]]
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[[Category: organic solvent]]
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[[Category: serine protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:10:18 2008''
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Current revision

CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG IN 40% ACETONITRILE

PDB ID 1bfk

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