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1tli

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[[Image:1tli.jpg|left|200px]]
 
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{{Structure
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==THERMOLYSIN (2% ISOPROPANOL SOAKED CRYSTALS)==
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|PDB= 1tli |SIZE=350|CAPTION= <scene name='initialview01'>1tli</scene>, resolution 2.05&Aring;
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<StructureSection load='1tli' size='340' side='right'caption='[[1tli]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=DMS:DIMETHYL SULFOXIDE'>DMS</scene>
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<table><tr><td colspan='2'>[[1tli]] 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=1TLI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TLI FirstGlance]. <br>
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|ACTIVITY= [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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
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|GENE=
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<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>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tli OCA], [https://pdbe.org/1tli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tli RCSB], [https://www.ebi.ac.uk/pdbsum/1tli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tli ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/THER_BACTH THER_BACTH] Extracellular zinc metalloprotease.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tl/1tli_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tli ConSurf].
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<div style="clear:both"></div>
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'''THERMOLYSIN (2% ISOPROPANOL SOAKED CRYSTALS)'''
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==See Also==
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*[[Thermolysin 3D structures|Thermolysin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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1TLI is a [[Single protein]] structure of 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=1TLI OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10651278 10651278]
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[[Category: Bacillus thermoproteolyticus]]
[[Category: Bacillus thermoproteolyticus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Thermolysin]]
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[[Category: Done SH]]
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[[Category: Done, S H.]]
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[[Category: English AC]]
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[[Category: English, A C.]]
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[[Category: Groom CR]]
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[[Category: Groom, C R.]]
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[[Category: Hubbard RE]]
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[[Category: Hubbard, R E.]]
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[[Category: CA]]
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[[Category: DMS]]
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[[Category: ZN]]
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[[Category: hydrolase]]
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[[Category: metalloproteinase]]
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[[Category: organic solvent]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:20:00 2008''
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Current revision

THERMOLYSIN (2% ISOPROPANOL SOAKED CRYSTALS)

PDB ID 1tli

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