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| | <StructureSection load='5onr' size='340' side='right'caption='[[5onr]], [[Resolution|resolution]] 1.39Å' scene=''> | | <StructureSection load='5onr' size='340' side='right'caption='[[5onr]], [[Resolution|resolution]] 1.39Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5onr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ONR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ONR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5onr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ONR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ONR 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=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.39Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5onp|5onp]], [[5onq|5onq]]</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=DMS:DIMETHYL+SULFOXIDE'>DMS</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/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] </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=5onr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5onr OCA], [https://pdbe.org/5onr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5onr RCSB], [https://www.ebi.ac.uk/pdbsum/5onr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5onr ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5onr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5onr OCA], [http://pdbe.org/5onr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5onr RCSB], [http://www.ebi.ac.uk/pdbsum/5onr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5onr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/THER_BACTH THER_BACTH]] Extracellular zinc metalloprotease. | + | [https://www.uniprot.org/uniprot/THER_BACTH THER_BACTH] Extracellular zinc metalloprotease. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Bacillus thermoproteolyticus]] | | [[Category: Bacillus thermoproteolyticus]] |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thermolysin]]
| + | [[Category: Gales L]] |
| - | [[Category: Gales, L]] | + | [[Category: Leite JP]] |
| - | [[Category: Leite, J P]] | + | |
| - | [[Category: Amyloid-beta peptide]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Peptidase]]
| + | |
| - | [[Category: Protein-peptide complex]]
| + | |
| Structural highlights
Function
THER_BACTH Extracellular zinc metalloprotease.
Publication Abstract from PubMed
The interaction of the amyloid-beta peptide (Abeta) with thermolysin (TLN) was investigated by X-ray crystallography. Structural models of the complexes of TLN with several Abeta fragments show that, despite the numerous possible cleavage sites of the Abeta sequence, the C-terminal product of Ala30-Ile31 cleavage does not dissociate, thus inhibiting the enzyme. The high similarity between the TLN structural motif and neprilysin (NEP), the most extensively studied peptidase associated with Abeta clearance, suggests that NEP should be more efficient against Abeta polymorphs where Ala30-Ile31 is inaccessible, which is in agreement with studies in living mice that point to the limited role of NEP in degrading soluble Abeta and its higher ability to degrade insoluble and/or oligomeric Abeta forms, producing only the Abeta10-37 intermediate.
Alzheimer's Abeta1-40 peptide degradation by thermolysin: evidence of inhibition by a C-terminal Abeta product.,Leite JP, Gales L FEBS Lett. 2019 Jan;593(1):128-137. doi: 10.1002/1873-3468.13285. Epub 2018 Nov, 23. PMID:30403288[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Leite JP, Gales L. Alzheimer's Abeta1-40 peptide degradation by thermolysin: evidence of inhibition by a C-terminal Abeta product. FEBS Lett. 2019 Jan;593(1):128-137. doi: 10.1002/1873-3468.13285. Epub 2018 Nov, 23. PMID:30403288 doi:http://dx.doi.org/10.1002/1873-3468.13285
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