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1qz3

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(New page: 200px<br /><applet load="1qz3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qz3, resolution 2.30&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1qz3.gif|left|200px]]<br /><applet load="1qz3" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qz3, resolution 2.30&Aring;" />
 
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'''CRYSTAL STRUCTURE OF MUTANT M211S/R215L OF CARBOXYLESTERASE EST2 COMPLEXED WITH HEXADECANESULFONATE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF MUTANT M211S/R215L OF CARBOXYLESTERASE EST2 COMPLEXED WITH HEXADECANESULFONATE==
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The reaction mechanism of the esterase 2 (EST2) from Alicyclobacillus, acidocaldarius was studied at the kinetic and structural level to shed, light on the mechanism of activity and substrate specificity increase, previously observed in its double mutant M211S/R215L. In particular, the, values of kinetic constants (k1, k(-1), k2, and k3) along with activation, energies (E1, E(-1), E2, and E3) were measured for wild type and mutant, enzyme. The previously suggested substrate-induced switch in the reaction, mechanism from kcat=k3 with a short acyl chain substrate (p-nitrophenyl, hexanoate) to kcat=k2 with a long acyl chain substrate (p-nitrophenyl, dodecanoate) was validated. The inhibition afforded by an irreversible, inhibitor (1-hexadecanesulfonyl chloride), structurally related to, p-nitrophenyl dodecanoate, was studied by kinetic analysis. Moreover the, three-dimensional structure of the double mutant bound to this inhibitor, was determined, providing essential information on the enzyme mechanism., In fact, structural analysis explained the observed substrate-induced, switch because of an inversion in the binding mode of the long acyl chain, derivatives with respect to the acyl- and alcohol-binding sites.
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<StructureSection load='1qz3' size='340' side='right'caption='[[1qz3]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qz3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QZ3 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=HDS:1-HEXADECANOSULFONIC+ACID'>HDS</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=1qz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qz3 OCA], [https://pdbe.org/1qz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qz3 RCSB], [https://www.ebi.ac.uk/pdbsum/1qz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qz3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q7SIG1_ALIAC Q7SIG1_ALIAC]
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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/qz/1qz3_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=1qz3 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 reaction mechanism of the esterase 2 (EST2) from Alicyclobacillus acidocaldarius was studied at the kinetic and structural level to shed light on the mechanism of activity and substrate specificity increase previously observed in its double mutant M211S/R215L. In particular, the values of kinetic constants (k1, k(-1), k2, and k3) along with activation energies (E1, E(-1), E2, and E3) were measured for wild type and mutant enzyme. The previously suggested substrate-induced switch in the reaction mechanism from kcat=k3 with a short acyl chain substrate (p-nitrophenyl hexanoate) to kcat=k2 with a long acyl chain substrate (p-nitrophenyl dodecanoate) was validated. The inhibition afforded by an irreversible inhibitor (1-hexadecanesulfonyl chloride), structurally related to p-nitrophenyl dodecanoate, was studied by kinetic analysis. Moreover the three-dimensional structure of the double mutant bound to this inhibitor was determined, providing essential information on the enzyme mechanism. In fact, structural analysis explained the observed substrate-induced switch because of an inversion in the binding mode of the long acyl chain derivatives with respect to the acyl- and alcohol-binding sites.
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==About this Structure==
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A substrate-induced switch in the reaction mechanism of a thermophilic esterase: kinetic evidences and structural basis.,De Simone G, Mandrich L, Menchise V, Giordano V, Febbraio F, Rossi M, Pedone C, Manco G J Biol Chem. 2004 Feb 20;279(8):6815-23. Epub 2003 Nov 15. PMID:14617621<ref>PMID:14617621</ref>
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1QZ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius] with HDS as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QZ3 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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A substrate-induced switch in the reaction mechanism of a thermophilic esterase: kinetic evidences and structural basis., De Simone G, Mandrich L, Menchise V, Giordano V, Febbraio F, Rossi M, Pedone C, Manco G, J Biol Chem. 2004 Feb 20;279(8):6815-23. Epub 2003 Nov 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14617621 14617621]
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</div>
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[[Category: Alicyclobacillus acidocaldarius]]
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<div class="pdbe-citations 1qz3" style="background-color:#fffaf0;"></div>
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[[Category: Carboxylesterase]]
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[[Category: Single protein]]
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[[Category: Febbraio, F.]]
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[[Category: Giordano, V.]]
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[[Category: Manco, G.]]
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[[Category: Mandrich, L.]]
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[[Category: Menchise, V.]]
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[[Category: Pedone, C.]]
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[[Category: Rossi, M.]]
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[[Category: Simone, G.De.]]
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[[Category: HDS]]
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[[Category: alpha/beta hydrolase fold]]
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[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 21:49:17 2007''
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==See Also==
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*[[Carboxylesterase 3D structures|Carboxylesterase 3D structures]]
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*[[Lipase 3D Structures|Lipase 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: Alicyclobacillus acidocaldarius]]
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[[Category: Large Structures]]
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[[Category: De Simone G]]
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[[Category: Febbraio F]]
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[[Category: Giordano V]]
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[[Category: Manco G]]
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[[Category: Mandrich L]]
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[[Category: Menchise V]]
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[[Category: Pedone C]]
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[[Category: Rossi M]]

Current revision

CRYSTAL STRUCTURE OF MUTANT M211S/R215L OF CARBOXYLESTERASE EST2 COMPLEXED WITH HEXADECANESULFONATE

PDB ID 1qz3

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