4dww: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<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> | <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" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SEB:O-BENZYLSULFONYL-SERINE'>SEB</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74Å</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='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='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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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 == | ||
Latest revision as of 16:44, 8 November 2023
Crystal Structure of Nattokinase from Bacillus subtilis nattoCrystal Structure of Nattokinase from Bacillus subtilis natto
Structural highlights
FunctionSUBN_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 PubMedNattokinase 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 AlsoReferences
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