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| | <StructureSection load='1zdp' size='340' side='right'caption='[[1zdp]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='1zdp' size='340' side='right'caption='[[1zdp]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zdp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/'bacillus_thermoproteolyticus' 'bacillus thermoproteolyticus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZDP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zdp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZDP 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=TIO:(2-MERCAPTOMETHYL-3-PHENYL-PROPIONYL)-GLYCINE'>TIO</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]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1z9g|1z9g]]</div></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=TIO:(2-MERCAPTOMETHYL-3-PHENYL-PROPIONYL)-GLYCINE'>TIO</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'>[https://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [https://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=1zdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zdp OCA], [https://pdbe.org/1zdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zdp RCSB], [https://www.ebi.ac.uk/pdbsum/1zdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zdp 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=1zdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zdp OCA], [https://pdbe.org/1zdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zdp RCSB], [https://www.ebi.ac.uk/pdbsum/1zdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zdp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/THER_BACTH THER_BACTH]] Extracellular zinc metalloprotease.
| + | [https://www.uniprot.org/uniprot/THER_BACTH THER_BACTH] Extracellular zinc metalloprotease. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Bacillus thermoproteolyticus]] | | [[Category: Bacillus thermoproteolyticus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thermolysin]]
| + | [[Category: Fournie-Zaluski MC]] |
| - | [[Category: Fournie-Zaluski, M C]] | + | [[Category: Matthews BW]] |
| - | [[Category: Matthews, B W]] | + | [[Category: Roderick SL]] |
| - | [[Category: Roderick, S L]] | + | [[Category: Roques BP]] |
| - | [[Category: Roques, B P]] | + | |
| - | [[Category: Enzyme-inhibitor complex]]
| + | |
| - | [[Category: Gamma turn]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Thermostable]]
| + | |
| - | [[Category: Zinc endopeptidase]]
| + | |
| Structural highlights
Function
THER_BACTH Extracellular zinc metalloprotease.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The three-dimensional structures of (S)-thiorphan and (R)-retro-thiorphan bound to thermolysin have been determined crystallographically and refined to residuals of 0.183 and 0.187 at 1.7-A resolution. Thiorphan [N-[(S)-2-(mercaptomethyl)-1-oxo-3-phenylpropyl]glycine] [HSCH2CH(CH2C6H5)CONHC-H2COOH] and retro-thiorphan [[[(R)-1-(mercaptomethyl)-2-phenylethyl] amino]-3-oxopropanoic acid] [HSCH2CH(CH2C6H5)NHCOCH2COOH] are isomeric thiol-containing inhibitors of endopeptidase EC 24-11 (also called "enkephalinase"). The mode of binding of thiorphan to thermolysin is similar to that of (2-benzyl-3-mercaptopropanoyl)-L-alanylglycinamide [Monzingo, A.F., & Matthews, B.W. (1982) Biochemistry 21, 3390-3394] with the inhibitor sulfur atom coordinated to the active site zinc and the peptide portion forming substrate-like interactions with the enzyme. The isomeric inhibitor retro-thiorphan, which differs from thiorphan by the inversion of an amide bond, utilizes very similar interactions with enzyme. Despite the inversion of the -CO-NH- linkage the carbonyl oxygen and amide nitrogen display very similar hydrogen bonding, as anticipated by B.P. Roques et al. [(1983) Proc. Natl. Acad. Sci. U.S.A. 80, 3178-3182]. These results explain why thermolysin and possibly other zinc endopeptidases such as endopeptidase EC 24-11 fail to discriminate between these retro-inverso inhibitors.
Thiorphan and retro-thiorphan display equivalent interactions when bound to crystalline thermolysin.,Roderick SL, Fournie-Zaluski MC, Roques BP, Matthews BW Biochemistry. 1989 Feb 21;28(4):1493-7. PMID:2719912[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Roderick SL, Fournie-Zaluski MC, Roques BP, Matthews BW. Thiorphan and retro-thiorphan display equivalent interactions when bound to crystalline thermolysin. Biochemistry. 1989 Feb 21;28(4):1493-7. PMID:2719912
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