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1hqd

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(New page: 200px<br /><applet load="1hqd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hqd, resolution 2.30&Aring;" /> '''PSEUDOMONAS CEPACIA ...)
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[[Image:1hqd.gif|left|200px]]<br /><applet load="1hqd" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hqd, resolution 2.30&Aring;" />
 
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'''PSEUDOMONAS CEPACIA LIPASE COMPLEXED WITH TRANSITION STATE ANALOGUE OF 1-PHENOXY-2-ACETOXY BUTANE'''<br />
 
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==Overview==
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==PSEUDOMONAS CEPACIA LIPASE COMPLEXED WITH TRANSITION STATE ANALOGUE OF 1-PHENOXY-2-ACETOXY BUTANE==
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In a series of four racemic phenoxyalkyl-alkyl carbinols, 1-phenoxy-2-hydroxybutane (1) is enantioselectively acetylated by, Burkholderia cepacia (formerly Pseudomonas cepacia) lipase with an E value, &gt; or = 200, whereas for the other three racemates E was found to be &lt; or =, 4. To explain the high preference of B. cepacia lipase for (R)-(+)-1, a, precursor of its transition state analogue with a tetrahedral P-atom, (R(P),S(P))-O-(2R)-(1-phenoxybut-2-yl)methylphosphonic acid chloride was, prepared and crystallized in complex with B. cepacia lipase. The X-ray, structure of the complex was determined, allowing to compare the, conformation of the inhibitor with results of molecular modelling.
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<StructureSection load='1hqd' size='340' side='right'caption='[[1hqd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hqd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HQD 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=INK:(RP,SP)-O-(2R)-(1-PHENOXYBUT-2-YL)-METHYLPHOSPHONIC+ACID+CHLORIDE'>INK</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=1hqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hqd OCA], [https://pdbe.org/1hqd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hqd RCSB], [https://www.ebi.ac.uk/pdbsum/1hqd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hqd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LIP_BURCE LIP_BURCE] Catalyzes the hydrolysis of triglycerides.
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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/hq/1hqd_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=1hqd 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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In a series of four racemic phenoxyalkyl-alkyl carbinols, 1-phenoxy-2-hydroxybutane (1) is enantioselectively acetylated by Burkholderia cepacia (formerly Pseudomonas cepacia) lipase with an E value &gt; or = 200, whereas for the other three racemates E was found to be &lt; or = 4. To explain the high preference of B. cepacia lipase for (R)-(+)-1, a precursor of its transition state analogue with a tetrahedral P-atom, (R(P),S(P))-O-(2R)-(1-phenoxybut-2-yl)methylphosphonic acid chloride was prepared and crystallized in complex with B. cepacia lipase. The X-ray structure of the complex was determined, allowing to compare the conformation of the inhibitor with results of molecular modelling.
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==About this Structure==
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Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane: biocatalytic, structural and modelling study.,Luic M, Tomic S, Lescic I, Ljubovic E, Sepac D, Sunjic V, Vitale L, Saenger W, Kojic-Prodic B Eur J Biochem. 2001 Jul;268(14):3964-73. PMID:11453990<ref>PMID:11453990</ref>
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1HQD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia] with CA and INK as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HQD 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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Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane: biocatalytic, structural and modelling study., Luic M, Tomic S, Lescic I, Ljubovic E, Sepac D, Sunjic V, Vitale L, Saenger W, Kojic-Prodic B, Eur J Biochem. 2001 Jul;268(14):3964-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11453990 11453990]
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</div>
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[[Category: Burkholderia cepacia]]
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<div class="pdbe-citations 1hqd" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Triacylglycerol lipase]]
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[[Category: Kojic-Prodic, B.]]
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[[Category: Lescic, I.]]
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[[Category: Ljubovic, E.]]
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[[Category: Luic, M.]]
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[[Category: Saenger, W.]]
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[[Category: Sepac, D.]]
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[[Category: Sunjic, V.]]
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[[Category: Tomic, S.]]
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[[Category: Vitale, L.]]
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[[Category: CA]]
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[[Category: INK]]
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[[Category: crystal structure]]
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[[Category: molecular modelling]]
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[[Category: pseudomonas cepacia lipase]]
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[[Category: racemic sec alcohols]]
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[[Category: transition state (ts) analogue]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:44:40 2007''
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==See Also==
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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: Burkholderia cepacia]]
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[[Category: Large Structures]]
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[[Category: Kojic-Prodic B]]
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[[Category: Lescic I]]
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[[Category: Ljubovic E]]
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[[Category: Luic M]]
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[[Category: Saenger W]]
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[[Category: Sepac D]]
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[[Category: Sunjic V]]
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[[Category: Tomic S]]
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[[Category: Vitale L]]

Current revision

PSEUDOMONAS CEPACIA LIPASE COMPLEXED WITH TRANSITION STATE ANALOGUE OF 1-PHENOXY-2-ACETOXY BUTANE

PDB ID 1hqd

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