1tlx

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[[Image:1tlx.jpg|left|200px]]<br /><applet load="1tlx" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1tlx, resolution 2.10&Aring;" />
 
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'''THERMOLYSIN (NATIVE)'''<br />
 
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==Overview==
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==THERMOLYSIN (NATIVE)==
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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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<StructureSection load='1tlx' size='340' side='right'caption='[[1tlx]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1tlx]] 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=1TLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TLX FirstGlance]. <br>
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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]] 2.1&#8491;</td></tr>
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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=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=VAL:VALINE'>VAL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=1tlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tlx OCA], [https://pdbe.org/1tlx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tlx RCSB], [https://www.ebi.ac.uk/pdbsum/1tlx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tlx 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/1tlx_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=1tlx ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1TLX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=DMS:'>DMS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TLX OCA].
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*[[Thermolysin 3D structures|Thermolysin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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 Feb 21 15:14:57 2008''
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Current revision

THERMOLYSIN (NATIVE)

PDB ID 1tlx

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