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| | <StructureSection load='4dww' size='340' side='right'caption='[[4dww]], [[Resolution|resolution]] 1.74Å' scene=''> | | <StructureSection load='4dww' size='340' side='right'caption='[[4dww]], [[Resolution|resolution]] 1.74Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4dww]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._natto Bacillus subtilis subsp. natto]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DWW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DWW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4dww]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._natto Bacillus subtilis subsp. natto]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DWW 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></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=SEB:O-BENZYLSULFONYL-SERINE'>SEB</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEB:O-BENZYLSULFONYL-SERINE'>SEB</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=4dww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dww OCA], [https://pdbe.org/4dww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dww RCSB], [https://www.ebi.ac.uk/pdbsum/4dww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dww 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>
| + | |
| - | <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=4dww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dww OCA], [http://pdbe.org/4dww PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dww RCSB], [http://www.ebi.ac.uk/pdbsum/4dww PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dww ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SUBN_BACNA SUBN_BACNA]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Subtilisin NAT also has fibrinolytic activity. | + | [[https://www.uniprot.org/uniprot/SUBN_BACNA SUBN_BACNA]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Subtilisin NAT also has fibrinolytic activity. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Subtilisin|Subtilisin]] | + | *[[Subtilisin 3D structures|Subtilisin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Bacillus subtilis subsp. natto]] | | [[Category: Bacillus subtilis subsp. natto]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Subtilisin]]
| + | [[Category: Chatake T]] |
| - | [[Category: Chatake, T]] | + | [[Category: Yanagisawa Y]] |
| - | [[Category: Yanagisawa, Y]] | + | |
| - | [[Category: Fibrinolytic activity]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
[SUBN_BACNA] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Subtilisin NAT also has fibrinolytic activity.
Publication Abstract from PubMed
Nattokinase is a single polypeptide chain composed of 275 amino acids (molecular weight 27,724) which displays strong fibrinolytic activity. Moreover, it can activate other fibrinolytic enzymes such as pro-urokinase and tissue plasminogen activator. In the present study, native nattokinase from Bacillus subtilis natto was purified using gel-filtration chromatography and crystallized to give needle-like crystals which could be used for X-ray diffraction experiments. The crystals belonged to space group C2, with unit-cell parameters a=74.3, b=49.9, c=56.3 A, beta=95.2 degrees . Diffraction images were processed to a resolution of 1.74 A with an Rmerge of 5.2% (15.3% in the highest resolution shell) and a completeness of 69.8% (30.0% in the highest resolution shell). This study reports the first X-ray diffraction analysis of nattokinase.
Purification, crystallization and preliminary X-ray diffraction experiment of nattokinase from Bacillus subtilis natto.,Yanagisawa Y, Chatake T, Chiba-Kamoshida K, Naito S, Ohsugi T, Sumi H, Yasuda I, Morimoto Y Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt 12):1670-3., Epub 2010 Nov 27. PMID:21139221[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yanagisawa Y, Chatake T, Chiba-Kamoshida K, Naito S, Ohsugi T, Sumi H, Yasuda I, Morimoto Y. Purification, crystallization and preliminary X-ray diffraction experiment of nattokinase from Bacillus subtilis natto. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt 12):1670-3., Epub 2010 Nov 27. PMID:21139221 doi:10.1107/S1744309110043137
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