2trm

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(New page: 200px<br /><applet load="2trm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2trm, resolution 2.8&Aring;" /> '''THE THREE-DIMENSIONAL...)
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[[Image:2trm.jpg|left|200px]]<br /><applet load="2trm" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2trm, resolution 2.8&Aring;" />
 
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'''THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS'''<br />
 
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==Overview==
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==THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS==
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The structure of the Asn102 mutant of trypsin was determined in order to, distinguish whether the reduced activity of the mutant at neutral pH, results from an altered active site conformation or from an inability to, stabilize a positive charge on the active site histidine. The active site, structure of the Asn102 mutant of trypsin is identical to the native, enzyme with respect to the specificity pocket, the oxyanion hole, and the, orientation of the nucleophilic serine. The observed decrease in rate, results from the loss of nucleophilicity of the active site serine. This, decreased nucleophilicity may result from stabilization of a His57, tautomer that is unable to accept the serine hydroxyl proton.
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<StructureSection load='2trm' size='340' side='right'caption='[[2trm]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2trm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TRM FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></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=2trm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2trm OCA], [https://pdbe.org/2trm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2trm RCSB], [https://www.ebi.ac.uk/pdbsum/2trm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2trm ProSAT]</span></td></tr>
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</table>
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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/tr/2trm_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=2trm 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 structure of the Asn102 mutant of trypsin was determined in order to distinguish whether the reduced activity of the mutant at neutral pH results from an altered active site conformation or from an inability to stabilize a positive charge on the active site histidine. The active site structure of the Asn102 mutant of trypsin is identical to the native enzyme with respect to the specificity pocket, the oxyanion hole, and the orientation of the nucleophilic serine. The observed decrease in rate results from the loss of nucleophilicity of the active site serine. This decreased nucleophilicity may result from stabilization of a His57 tautomer that is unable to accept the serine hydroxyl proton.
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==About this Structure==
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The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis.,Sprang S, Standing T, Fletterick RJ, Stroud RM, Finer-Moore J, Xuong NH, Hamlin R, Rutter WJ, Craik CS Science. 1987 Aug 21;237(4817):905-9. PMID:3112942<ref>PMID:3112942</ref>
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2TRM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA and BEN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2TRM 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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The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis., Sprang S, Standing T, Fletterick RJ, Stroud RM, Finer-Moore J, Xuong NH, Hamlin R, Rutter WJ, Craik CS, Science. 1987 Aug 21;237(4817):905-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3112942 3112942]
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</div>
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[[Category: Rattus norvegicus]]
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<div class="pdbe-citations 2trm" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Trypsin]]
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[[Category: Finer-Moore, J.]]
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[[Category: Stroud, R.M.]]
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[[Category: BEN]]
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[[Category: CA]]
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[[Category: hydrolase (serine proteinase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 14:06:18 2007''
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==See Also==
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*[[Trypsin 3D structures|Trypsin 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: Buffalo rat]]
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[[Category: Large Structures]]
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[[Category: Trypsin]]
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[[Category: Finer-Moore, J]]
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[[Category: Stroud, R M]]

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THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS

PDB ID 2trm

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