1be6

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[[Image:1be6.gif|left|200px]]
 
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==TRANS-CINNAMOYL-SUBTILISIN IN ANHYDROUS ACETONITRILE==
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The line below this paragraph, containing "STRUCTURE_1be6", creates the "Structure Box" on the page.
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<StructureSection load='1be6' size='340' side='right'caption='[[1be6]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1be6]] 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=1BE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BE6 FirstGlance]. <br>
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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]] 2.15&#8491;</td></tr>
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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>, <scene name='pdbligand=TCA:PHENYLETHYLENECARBOXYLIC+ACID'>TCA</scene></td></tr>
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{{STRUCTURE_1be6| PDB=1be6 | SCENE= }}
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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=1be6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1be6 OCA], [https://pdbe.org/1be6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1be6 RCSB], [https://www.ebi.ac.uk/pdbsum/1be6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1be6 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 (PubMed:11109488, Ref.4). 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/be/1be6_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1be6 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 trans-cinnamoyl-subtilisin, an acyl-enzyme covalent intermediate of the serine protease subtilisin Carlsberg, have been determined to 2.2-A resolution in anhydrous acetonitrile and in water. The cinnamoyl-subtilisin structures are virtually identical in the two solvents. In addition, their enzyme portions are nearly indistinguishable from previously determined structures of the free enzyme in acetonitrile and in water; thus, acylation in either aqueous or nonaqueous solvent causes no appreciable conformational changes. However, the locations of bound solvent molecules in the active site of the acyl- and free enzyme forms in acetonitrile and in water are distinct. Such differences in the active site solvation may contribute to the observed variations in enzymatic activities. On prolonged exposure to organic solvent or removal of interstitial solvent from the crystal lattice, the channels within enzyme crystals are shown to collapse, leading to a drop in the number of active sites accessible to the substrate. The mechanistic and preparative implications of our findings for enzymatic catalysis in organic solvents are discussed.
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'''TRANS-CINNAMOYL-SUBTILISIN IN ANHYDROUS ACETONITRILE'''
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Comparison of x-ray crystal structures of an acyl-enzyme intermediate of subtilisin Carlsberg formed in anhydrous acetonitrile and in water.,Schmitke JL, Stern LJ, Klibanov AM Proc Natl Acad Sci U S A. 1998 Oct 27;95(22):12918-23. PMID:9789015<ref>PMID:9789015</ref>
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==Overview==
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The x-ray crystal structures of trans-cinnamoyl-subtilisin, an acyl-enzyme covalent intermediate of the serine protease subtilisin Carlsberg, have been determined to 2.2-A resolution in anhydrous acetonitrile and in water. The cinnamoyl-subtilisin structures are virtually identical in the two solvents. In addition, their enzyme portions are nearly indistinguishable from previously determined structures of the free enzyme in acetonitrile and in water; thus, acylation in either aqueous or nonaqueous solvent causes no appreciable conformational changes. However, the locations of bound solvent molecules in the active site of the acyl- and free enzyme forms in acetonitrile and in water are distinct. Such differences in the active site solvation may contribute to the observed variations in enzymatic activities. On prolonged exposure to organic solvent or removal of interstitial solvent from the crystal lattice, the channels within enzyme crystals are shown to collapse, leading to a drop in the number of active sites accessible to the substrate. The mechanistic and preparative implications of our findings for enzymatic catalysis in organic solvents are discussed.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1BE6 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=1BE6 OCA].
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</div>
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<div class="pdbe-citations 1be6" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Comparison of x-ray crystal structures of an acyl-enzyme intermediate of subtilisin Carlsberg formed in anhydrous acetonitrile and in water., Schmitke JL, Stern LJ, Klibanov AM, Proc Natl Acad Sci U S A. 1998 Oct 27;95(22):12918-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9789015 9789015]
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*[[Subtilisin 3D structures|Subtilisin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[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: Acyl-enzyme]]
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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 Fri May 2 11:23:57 2008''
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Current revision

TRANS-CINNAMOYL-SUBTILISIN IN ANHYDROUS ACETONITRILE

PDB ID 1be6

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