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1hyt

From Proteopedia

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[[Image:1hyt.gif|left|200px]]<br /><applet load="1hyt" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hyt, resolution 1.70&Aring;" />
 
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'''RE-DETERMINATION AND REFINEMENT OF THE COMPLEX OF BENZYLSUCCINIC ACID WITH THERMOLYSIN AND ITS RELATION TO THE COMPLEX WITH CARBOXYPEPTIDASE A'''<br />
 
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==Overview==
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==RE-DETERMINATION AND REFINEMENT OF THE COMPLEX OF BENZYLSUCCINIC ACID WITH THERMOLYSIN AND ITS RELATION TO THE COMPLEX WITH CARBOXYPEPTIDASE A==
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The complex of benzylsuccinic acid with thermolysin has been redetermined at 1.7-A resolution and refined to a crystallographic residual of 15.7%. In contrast to the prior study, which was to 2.3-A resolution, and without the benefit of refinement (Bolognesi, M. C. and Matthews, B. W. (1979) J. Biol. Chem. 254, 634-639), the present analysis shows that it is the D- rather than the L-isomer of benzylsuccinic acid that binds. The stereochemistry of the zinc-carboxylate interaction is now seen to be syn, as is also observed in all known zinc-carboxylate complexes of both thermolysin and carboxypeptidase A. The mode of binding of the beta-carboxylate resembles the presumed geometry of the tetrahedral transition state and, as such, is consistent with the commonly accepted mechanism of action of thermolysin and of carboxypeptidase A.
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<StructureSection load='1hyt' size='340' side='right'caption='[[1hyt]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hyt]] 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=1HYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HYT 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]] 1.7&#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=BZS:L-BENZYLSUCCINIC+ACID'>BZS</scene>, <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>
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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=1hyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyt OCA], [https://pdbe.org/1hyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hyt RCSB], [https://www.ebi.ac.uk/pdbsum/1hyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hyt 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/hy/1hyt_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=1hyt 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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1HYT 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=CA:'>CA</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=DMS:'>DMS</scene> and <scene name='pdbligand=BZS:'>BZS</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=1HYT 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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Redetermination and refinement of the complex of benzylsuccinic acid with thermolysin and its relation to the complex with carboxypeptidase A., Hausrath AC, Matthews BW, J Biol Chem. 1994 Jul 22;269(29):18839-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8034637 8034637]
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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: Hausrath AC]]
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[[Category: Hausrath, A C.]]
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[[Category: Matthews BW]]
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[[Category: Matthews, B W.]]
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[[Category: BZS]]
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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://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:10 2008''
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Current revision

RE-DETERMINATION AND REFINEMENT OF THE COMPLEX OF BENZYLSUCCINIC ACID WITH THERMOLYSIN AND ITS RELATION TO THE COMPLEX WITH CARBOXYPEPTIDASE A

PDB ID 1hyt

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