1tli

<StructureSection load='1tli' size='340' side='right' caption='[[1tli]], [[Resolution|resolution]] 2.05&Aring;' scene=''>

<table><tr><td colspan='2'>[[1tli]] 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=1TLI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TLI FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>

<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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tli OCA], [http://pdbe.org/1tli PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tli RCSB], [http://www.ebi.ac.uk/pdbsum/1tli PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tli ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/THER_BACTH THER_BACTH]] Extracellular zinc metalloprotease.

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== 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<ref>PMID:10651278</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1tli" style="background-color:#fffaf0;"></div>

*[[Thermolysin|Thermolysin]]

[[Category: Thermolysin]]

[[Category: Done, S H]]

[[Category: English, A C]]

[[Category: Groom, C R]]

[[Category: Hubbard, R E]]

[[Category: Organic solvent]]