2tlx

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[[Image:2tlx.jpg|left|200px]]
 
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{{Structure
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==THERMOLYSIN (NATIVE)==
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|PDB= 2tlx |SIZE=350|CAPTION= <scene name='initialview01'>2tlx</scene>, resolution 1.65&Aring;
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<StructureSection load='2tlx' size='340' side='right'caption='[[2tlx]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[2tlx]] 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=2TLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TLX FirstGlance]. <br>
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|ACTIVITY= <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>
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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]] 1.65&#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=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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|DOMAIN=
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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=2tlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tlx OCA], [https://pdbe.org/2tlx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2tlx RCSB], [https://www.ebi.ac.uk/pdbsum/2tlx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2tlx ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1tlx|1TLX]], [[1tli|1TLI]], [[2tli|2TLI]], [[3tli|3TLI]], [[4tli|4TLI]], [[5tli|5TLI]], [[6tli|6TLI]], [[7tli|7TLI]], [[8tli|8TLI]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2tlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tlx OCA], [http://www.ebi.ac.uk/pdbsum/2tlx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2tlx RCSB]</span>
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== Function ==
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}}
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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/2tlx_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=2tlx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''THERMOLYSIN (NATIVE)'''
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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:10651278<ref>PMID:10651278</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2tlx" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Thermolysin 3D structures|Thermolysin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2TLX 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=2TLX OCA].
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__TOC__
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</StructureSection>
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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: 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 Mon Mar 31 05:03:50 2008''
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Current revision

THERMOLYSIN (NATIVE)

PDB ID 2tlx

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