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| | <StructureSection load='5tli' size='340' side='right'caption='[[5tli]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5tli' size='340' side='right'caption='[[5tli]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5tli]] is a 1 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=5TLI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TLI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5tli]] 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=5TLI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TLI 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=IPA:ISOPROPYL+ALCOHOL'>IPA</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tlx|1tlx]], [[2tlx|2tlx]], [[1tli|1tli]], [[2tli|2tli]], [[3tli|3tli]], [[4tli|4tli]], [[6tli|6tli]], [[7tli|7tli]], [[8tli|8tli]]</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=IPA:ISOPROPYL+ALCOHOL'>IPA</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=5tli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tli OCA], [https://pdbe.org/5tli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tli RCSB], [https://www.ebi.ac.uk/pdbsum/5tli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tli 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=5tli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tli OCA], [http://pdbe.org/5tli PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tli RCSB], [http://www.ebi.ac.uk/pdbsum/5tli PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tli 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. |
| | == 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: Done SH]] |
| - | [[Category: Done, S H]] | + | [[Category: English AC]] |
| - | [[Category: English, A C]] | + | [[Category: Groom CR]] |
| - | [[Category: Groom, C R]] | + | [[Category: Hubbard RE]] |
| - | [[Category: Hubbard, R E]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Metalloproteinase]]
| + | |
| - | [[Category: Organic solvent]]
| + | |
| 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
Multiple-solvent crystal structure determination (MSCS) allows the position and orientation of bound solvent fragments to be identified by determining the structure of protein crystals soaked in organic solvents. We have extended this technique by the determination of high-resolution crystal structures of thermolysin (TLN), generated from crystals soaked in 2% to 100% isopropanol. The procedure causes only minor changes to the conformation of the protein, and an increasing number of isopropanol interaction sites could be identified as the solvent concentration is increased. Isopropanol occupies all four of the main subsites in the active site, although this was only observed at very high concentrations of isopropanol for three of the four subsites. Analysis of the isopropanol positions shows little correlation with interaction energy computed using a molecular mechanics force field, but the experimentally determined positions of isopropanol are consistent with the structures of known protein-ligand complexes of TLN.
Locating interaction sites on proteins: the crystal structure of thermolysin soaked in 2% to 100% isopropanol.,English AC, Done SH, Caves LS, Groom CR, Hubbard RE Proteins. 1999 Dec 1;37(4):628-40. PMID:10651278[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ English AC, Done SH, Caves LS, Groom CR, Hubbard RE. Locating interaction sites on proteins: the crystal structure of thermolysin soaked in 2% to 100% isopropanol. Proteins. 1999 Dec 1;37(4):628-40. PMID:10651278
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