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| <StructureSection load='4cfy' size='340' side='right'caption='[[4cfy]], [[Resolution|resolution]] 1.17Å' scene=''> | | <StructureSection load='4cfy' size='340' side='right'caption='[[4cfy]], [[Resolution|resolution]] 1.17Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4cfy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10840 Atcc 10840]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CFY FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4cfy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lederbergia_lenta Lederbergia lenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CFY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CFY FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cfz|4cfz]], [[4cg0|4cg0]]</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=4cfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cfy OCA], [https://pdbe.org/4cfy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cfy RCSB], [https://www.ebi.ac.uk/pdbsum/4cfy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cfy ProSAT]</span></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cfy OCA], [http://pdbe.org/4cfy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cfy RCSB], [http://www.ebi.ac.uk/pdbsum/4cfy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cfy ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/SUBS_BACLE SUBS_BACLE]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. | | [[https://www.uniprot.org/uniprot/SUBS_LEDLE SUBS_LEDLE]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| A microcrystalline suspension of Bacillus lentus subtilisin (Savinase) produced during industrial large-scale production was analysed by X-ray powder diffraction (XRPD) and X-ray single-crystal diffraction (MX). XRPD established that the bulk microcrystal sample representative of the entire production suspension corresponded to space group P212121, with unit-cell parameters a = 47.65, b = 62.43, c = 75.74 A, equivalent to those for a known orthorhombic crystal form (PDB entry 1ndq). MX using synchrotron beamlines at the Diamond Light Source with beam dimensions of 20 x 20 microm was subsequently used to study the largest crystals present in the suspension, with diffraction data being collected from two single crystals ( approximately 20 x 20 x 60 microm) to resolutions of 1.40 and 1.57 A, respectively. Both structures also belonged to space group P212121, but were quite distinct from the dominant form identified by XRPD, with unit-cell parameters a = 53.04, b = 57.55, c = 71.37 A and a = 52.72, b = 57.13, c = 65.86 A, respectively, and refined to R = 10.8% and Rfree = 15.5% and to R = 14.1% and Rfree = 18.0%, respectively. They are also different from any of the forms previously reported in the PDB. A controlled crystallization experiment with a highly purified Savinase sample allowed the growth of single crystals of the form identified by XRPD; their structure was solved and refined to a resolution of 1.17 A with an R of 9.2% and an Rfree of 11.8%. Thus, there are at least three polymorphs present in the production suspension, albeit with the 1ndq-like microcrystals predominating. It is shown how the two techniques can provide invaluable and complementary information for such a production suspension and it is proposed that XRPD provides an excellent quality-control tool for such suspensions.
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| Analysis of an industrial production suspension of Bacillus lentus subtilisin crystals by powder diffraction: a powerful quality-control tool.,Frankaer CG, Moroz OV, Turkenburg JP, Aspmo SI, Thymark M, Friis EP, Stahl K, Nielsen JE, Wilson KS, Harris P Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):1115-23. doi:, 10.1107/S1399004714001497. Epub 2014 Mar 21. PMID:24699655<ref>PMID:24699655</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4cfy" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Subtilisin|Subtilisin]] | | *[[Subtilisin 3D structures|Subtilisin 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Atcc 10840]]
| |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Subtilisin]] | | [[Category: Lederbergia lenta]] |
| [[Category: Aspmo, S I]] | | [[Category: Aspmo SI]] |
| [[Category: Frankaer, C G]] | | [[Category: Frankaer CG]] |
| [[Category: Friis, E P]] | | [[Category: Friis EP]] |
| [[Category: Harris, P]] | | [[Category: Harris P]] |
| [[Category: Moroz, O V]] | | [[Category: Moroz OV]] |
| [[Category: Nielsen, J E]] | | [[Category: Nielsen JE]] |
| [[Category: Stahla, K]] | | [[Category: Stahla K]] |
| [[Category: Thymark, M]] | | [[Category: Thymark M]] |
| [[Category: Turkenburg, J P]] | | [[Category: Turkenburg JP]] |
| [[Category: Wilson, K S]] | | [[Category: Wilson KS]] |
| [[Category: Hydrolase]]
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| [[Category: Microcrystalline suspension]]
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| [[Category: Powder diffraction]]
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| [[Category: Quality control]]
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| [[Category: Single crystal analysis]]
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| [[Category: Subtilisin savinase]]
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