8tln

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(New page: 200px<br /><applet load="8tln" size="450" color="white" frame="true" align="right" spinBox="true" caption="8tln, resolution 1.6&Aring;" /> '''STRUCTURAL COMPARISON...)
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[[Image:8tln.gif|left|200px]]<br /><applet load="8tln" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="8tln, resolution 1.6&Aring;" />
 
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'''STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING CATALYSIS'''<br />
 
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==Overview==
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==STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING CATALYSIS==
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Crystal structures are known for three members of the bacterial neutral, protease family: thermolysin from Bacillus thermoproteolyticus (TLN), the, neutral protease from Bacillus cereus (NEU), and the elastase of, Pseudomonas aeruginosa (PAE), both in free and ligand-bound forms. Each, enzyme consists of an N-terminal and C-terminal domain with the active, site formed at the junction of the two domains. Comparison of the, different molecules reveals that the structure within each domain is well, conserved, but there are substantial hinge-bending displacements (up to 16, degrees) of one domain relative to the other. These domain motions can be, correlated with the presence or absence of bound inhibitor, as was, previously observed in the specific example of PAE [Thayer, M.M., Flaherty, K.M., &amp; McKay, D.B. (1991) J. Biol. Chem. 266, 2864-2871]. The, binding of inhibitor appears to be associated with a reduction of the, domain hinge-bending angle by 6-14 degrees and a closure of the "jaws" of, the active site cleft by about 2 A. Crystallographic refinement of the, structure of thermolysin suggests that electron density seen in the active, site of the enzyme in the original structure determination probably, corresponds to a bound dipeptide. Thus, the crystal structure appears to, correspond to an enzyme-inhibitor or enzyme-product complex, rather than, the free enzyme, as has previously been assumed.
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<StructureSection load='8tln' size='340' side='right'caption='[[8tln]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8tln]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3tln 3tln], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tln 1tln] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2tln 2tln]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8TLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TLN 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]] 1.6&#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=8tln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8tln OCA], [https://pdbe.org/8tln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8tln RCSB], [https://www.ebi.ac.uk/pdbsum/8tln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8tln 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/8tln_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=8tln 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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8TLN 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, ZN and DMS as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entries 3TLN, 1TLN and 2TLN. 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=8TLN 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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Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis., Holland DR, Tronrud DE, Pley HW, Flaherty KM, Stark W, Jansonius JN, McKay DB, Matthews BW, Biochemistry. 1992 Nov 24;31(46):11310-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1445869 1445869]
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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: Matthews BW]]
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[[Category: Matthews, B.W.]]
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[[Category: Tronrud D]]
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[[Category: Tronrud, D.]]
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[[Category: CA]]
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[[Category: DMS]]
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[[Category: ZN]]
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[[Category: hydrolase(metalloproteinase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:01:33 2007''
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Current revision

STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING CATALYSIS

PDB ID 8tln

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