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| | <StructureSection load='4ger' size='340' side='right'caption='[[4ger]], [[Resolution|resolution]] 1.59Å' scene=''> | | <StructureSection load='4ger' size='340' side='right'caption='[[4ger]], [[Resolution|resolution]] 1.59Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ger]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"aerobacillus_polymyxa"_(prazmowski_1880)_donker_1926 "aerobacillus polymyxa" (prazmowski 1880) donker 1926]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GER OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GER FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ger]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_polymyxa Paenibacillus polymyxa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GER 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=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=THR:THREONINE'>THR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=THR:THREONINE'>THR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.25, 3.4.24.26, 3.4.24.27, 3.4.24.28, 3.4.24.29, 3.4.24.30, 3.4.24.31, 3.4.24.32, 3.4.24.39 and 3.4.24.40 3.4.24.25, 3.4.24.26, 3.4.24.27, 3.4.24.28, 3.4.24.29, 3.4.24.30, 3.4.24.31, 3.4.24.32, 3.4.24.39 and 3.4.24.40] </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=4ger FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ger OCA], [https://pdbe.org/4ger PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ger RCSB], [https://www.ebi.ac.uk/pdbsum/4ger PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ger ProSAT]</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=4ger FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ger OCA], [http://pdbe.org/4ger PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ger RCSB], [http://www.ebi.ac.uk/pdbsum/4ger PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ger ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/NPRE_PAEPO NPRE_PAEPO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hydrolase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Benz, J]] | + | [[Category: Paenibacillus polymyxa]] |
| - | [[Category: Ruf, A]] | + | [[Category: Benz J]] |
| - | [[Category: Schmidt, M]] | + | [[Category: Ruf A]] |
| - | [[Category: Sobek, H]] | + | [[Category: Schmidt M]] |
| - | [[Category: Stihle, M]] | + | [[Category: Sobek H]] |
| - | [[Category: Metalloproteinase]]
| + | [[Category: Stihle M]] |
| - | [[Category: Protease]]
| + | |
| - | [[Category: Thermolysin-like protease]]
| + | |
| - | [[Category: Tissue disaggregation]]
| + | |
| Structural highlights
Function
NPRE_PAEPO
Publication Abstract from PubMed
Gentlyase is a bacterial extracellular metalloprotease that is widely applied in cell culture and for tissue dissociation and that belongs to the family of thermolysin-like proteases. The structure of thermolysin has been known since 1972 and that of Bacillus cereus neutral protease since 1992. However, the structure determination of other Bacillus neutral proteases has been hindered by their tendency to cannibalistic autolysis. High calcium conditions that allow the concentration and crystallization of the active Gentlyase metalloprotease without autoproteolysis were identified using thermal fluorescent shift assays. X-ray structures of the protease were solved in the absence and in the presence of the inhibitor phosphoramidon at 1.59 and 1.76 A resolution, respectively. No domain movement was observed upon inhibitor binding, although such movement is thought to be a general feature of the thermolysin-like protease family. Further analysis of the structure shows that the observed calcium dependency of Gentlyase stability may arise from a partly degenerated calcium site Ca1-2 and a deletion near site Ca3.
Structure of Gentlyase, the neutral metalloprotease of Paenibacillus polymyxa.,Ruf A, Stihle M, Benz J, Schmidt M, Sobek H Acta Crystallogr D Biol Crystallogr. 2013 Jan;69(Pt 1):24-31. doi:, 10.1107/S0907444912041169. Epub 2012 Dec 20. PMID:23275160[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ruf A, Stihle M, Benz J, Schmidt M, Sobek H. Structure of Gentlyase, the neutral metalloprotease of Paenibacillus polymyxa. Acta Crystallogr D Biol Crystallogr. 2013 Jan;69(Pt 1):24-31. doi:, 10.1107/S0907444912041169. Epub 2012 Dec 20. PMID:23275160 doi:10.1107/S0907444912041169
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