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New page: left|200px<br /><applet load="1hqd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hqd, resolution 2.30Å" /> '''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"
caption="1hqd, resolution 2.30&Aring;" />
'''PSEUDOMONAS CEPACIA LIPASE COMPLEXED WITH TRANSITION STATE ANALOGUE OF 1-PHENOXY-2-ACETOXY BUTANE'''<br />


==Overview==
==PSEUDOMONAS CEPACIA LIPASE COMPLEXED WITH TRANSITION STATE ANALOGUE OF 1-PHENOXY-2-ACETOXY BUTANE==
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.
<StructureSection load='1hqd' size='340' side='right'caption='[[1hqd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LIP_BURCE LIP_BURCE] Catalyzes the hydrolysis of triglycerides.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hq/1hqd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==About this Structure==
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>
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].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
<div class="pdbe-citations 1hqd" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Lipase 3D Structures|Lipase 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Burkholderia cepacia]]
[[Category: Burkholderia cepacia]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Triacylglycerol lipase]]
[[Category: Kojic-Prodic B]]
[[Category: Kojic-Prodic, B.]]
[[Category: Lescic I]]
[[Category: Lescic, I.]]
[[Category: Ljubovic E]]
[[Category: Ljubovic, E.]]
[[Category: Luic M]]
[[Category: Luic, M.]]
[[Category: Saenger W]]
[[Category: Saenger, W.]]
[[Category: Sepac D]]
[[Category: Sepac, D.]]
[[Category: Sunjic V]]
[[Category: Sunjic, V.]]
[[Category: Tomic S]]
[[Category: Tomic, S.]]
[[Category: Vitale L]]
[[Category: Vitale, L.]]
[[Category: CA]]
[[Category: INK]]
[[Category: crystal structure]]
[[Category: molecular modelling]]
[[Category: pseudomonas cepacia lipase]]
[[Category: racemic sec alcohols]]
[[Category: transition state (ts) analogue]]
 
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