1l3f

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(New page: 200px<br /><applet load="1l3f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l3f, resolution 2.3&Aring;" /> '''Thermolysin in the Ab...)
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[[Image:1l3f.gif|left|200px]]<br /><applet load="1l3f" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1l3f, resolution 2.3&Aring;" />
 
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'''Thermolysin in the Absence of Substrate has an Open Conformation'''<br />
 
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==Overview==
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==Thermolysin in the Absence of Substrate has an Open Conformation==
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The bacterial neutral proteases have been proposed to undergo, hinge-bending during their catalytic cycle. However, in thermolysin, the, prototypical member of the family, no significant conformational change, has been observed. The structure of thermolysin has now been determined in, a new crystal form that for the first time shows the enzyme in the absence, of a ligand bound in the active site. This is shown to be an 'open' form, of the enzyme. The relative orientation of the two domains that define the, active-site cleft differ by a 5 degrees rotation relative to their, positions in the previously studied ligand-bound 'closed' form. Based on, structural comparisons, kinetic studies on mutants and molecular-dynamics, simulations, Gly78 and Gly135-Gly136 have previously been suggested as two, possible hinge regions. Comparison of the 'open' and 'closed' structures, suggests that neither of the proposed hinge regions completely accounts, for the observed displacement. The concerted movement of a group of side, chains suggested to be associated with the hinge-bending motion is, however, confirmed.
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<StructureSection load='1l3f' size='340' side='right'caption='[[1l3f]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1l3f]] 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=1L3F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L3F 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]] 2.3&#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=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=1l3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l3f OCA], [https://pdbe.org/1l3f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l3f RCSB], [https://www.ebi.ac.uk/pdbsum/1l3f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l3f 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/l3/1l3f_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=1l3f 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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The bacterial neutral proteases have been proposed to undergo hinge-bending during their catalytic cycle. However, in thermolysin, the prototypical member of the family, no significant conformational change has been observed. The structure of thermolysin has now been determined in a new crystal form that for the first time shows the enzyme in the absence of a ligand bound in the active site. This is shown to be an 'open' form of the enzyme. The relative orientation of the two domains that define the active-site cleft differ by a 5 degrees rotation relative to their positions in the previously studied ligand-bound 'closed' form. Based on structural comparisons, kinetic studies on mutants and molecular-dynamics simulations, Gly78 and Gly135-Gly136 have previously been suggested as two possible hinge regions. Comparison of the 'open' and 'closed' structures suggests that neither of the proposed hinge regions completely accounts for the observed displacement. The concerted movement of a group of side chains suggested to be associated with the hinge-bending motion is, however, confirmed.
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==About this Structure==
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Thermolysin in the absence of substrate has an open conformation.,Hausrath AC, Matthews BW Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1002-7. Epub, 2002 May 29. PMID:12037302<ref>PMID:12037302</ref>
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1L3F 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 CA and ZN 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L3F OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Thermolysin in the absence of substrate has an open conformation., Hausrath AC, Matthews BW, Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1002-7. Epub, 2002 May 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12037302 12037302]
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</div>
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[[Category: Bacillus thermoproteolyticus]]
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<div class="pdbe-citations 1l3f" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Thermolysin]]
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[[Category: Hausrath, A.C.]]
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[[Category: Matthews, B.W.]]
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[[Category: CA]]
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[[Category: ZN]]
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[[Category: hinge-bending]]
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[[Category: hydrolase]]
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[[Category: matrix metalloprotease]]
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[[Category: thermolysin]]
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[[Category: zinc metalloprotease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:13:04 2007''
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==See Also==
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*[[Thermolysin 3D structures|Thermolysin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus thermoproteolyticus]]
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[[Category: Large Structures]]
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[[Category: Hausrath AC]]
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[[Category: Matthews BW]]

Current revision

Thermolysin in the Absence of Substrate has an Open Conformation

PDB ID 1l3f

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