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[[Image:5lip.gif|left|200px]]


{{Structure
==PSEUDOMONAS LIPASE COMPLEXED WITH RC-(RP, SP)-1,2-DIOCTYLCARBAMOYLGLYCERO-3-O-OCTYLPHOSPHONATE==
|PDB= 5lip |SIZE=350|CAPTION= <scene name='initialview01'>5lip</scene>, resolution 2.9&Aring;
<StructureSection load='5lip' size='340' side='right'caption='[[5lip]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
|SITE= <scene name='pdbsite=ACT:Active+Site'>ACT</scene> and <scene name='pdbsite=OXY:Oxyanion+Hole'>OXY</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=OCP:OCTYL-PHOSPHINIC+ACID+1,2-BIS-OCTYLCARBAMOYLOXY-ETHYL+ESTER'>OCP</scene>
<table><tr><td colspan='2'>[[5lip]] 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=5LIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LIP FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
|GENE=
<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=OCP:OCTYL-PHOSPHINIC+ACID+1,2-BIS-OCTYLCARBAMOYLOXY-ETHYL+ESTER'>OCP</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5lip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lip OCA], [https://pdbe.org/5lip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lip RCSB], [https://www.ebi.ac.uk/pdbsum/5lip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lip ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5lip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lip OCA], [http://www.ebi.ac.uk/pdbsum/5lip PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=5lip RCSB]</span>
== 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/li/5lip_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=5lip ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
To investigate the enantioselectivity of Pseudomonas cepacia lipase, inhibition studies were performed with Sc- and Rc-(Rp,Sp)-1,2-dialkylcarbamoylglycero-3-O-p-nitrophenyl alkylphosphonates of different alkyl chain lengths. P. cepacia lipase was most rapidly inactivated by Rc-(Rp,Sp)-1,2-dioctylcarbamoylglycero-3-O-p-nitrophenyl octylphosphonate (Rc-trioctyl) with an inactivation half-time of 75 min, while that for the Sc-(Rp,Sp)-1,2-dioctylcarbamoylglycero-3-O-p-nitrophenyl octyl-phosphonate (Sc-trioctyl) compound was 530 min. X-ray structures were obtained of P. cepacia lipase after reaction with Rc-trioctyl to 0.29-nm resolution at pH 4 and covalently modified with Rc-(Rp,Sp)-1,2-dibutylcarbamoylglycero-3-O-p-nitrophenyl butyl-phosphonate (Rc-tributyl) to 0.175-nm resolution at pH 8.5. The three-dimensional structures reveal that both triacylglycerol analogues had reacted with the active-site Ser87, forming a covalent complex. The bound phosphorus atom shows the same chirality (Sp) in both complexes despite the use of a racemic (Rp,Sp) mixture at the phosphorus atom of the triacylglycerol analogues. In the structure of Rc-tributyl-complexed P. cepacia lipase, the diacylglycerol moiety has been lost due to an aging reaction, and only the butyl phosphonate remains visible in the electron density. In the Rc-trioctyl complex the complete inhibitor is clearly defined; it adopts a bent tuning fork conformation. Unambiguously, four binding pockets for the triacylglycerol could be detected: an oxyanion hole and three pockets which accommodate the sn-1, sn-2, and sn-3 fatty acid chains. Van der Waals' interactions are the main forces that keep the radyl groups of the triacylglycerol analogue in position and, in addition, a hydrogen bond to the carbonyl oxygen of the sn-2 chain contributes to fixing the position of the inhibitor.


'''PSEUDOMONAS LIPASE COMPLEXED WITH RC-(RP, SP)-1,2-DIOCTYLCARBAMOYLGLYCERO-3-O-OCTYLPHOSPHONATE'''
Structural basis of the chiral selectivity of Pseudomonas cepacia lipase.,Lang DA, Mannesse ML, de Haas GH, Verheij HM, Dijkstra BW Eur J Biochem. 1998 Jun 1;254(2):333-40. PMID:9660188<ref>PMID:9660188</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lip" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
To investigate the enantioselectivity of Pseudomonas cepacia lipase, inhibition studies were performed with Sc- and Rc-(Rp,Sp)-1,2-dialkylcarbamoylglycero-3-O-p-nitrophenyl alkylphosphonates of different alkyl chain lengths. P. cepacia lipase was most rapidly inactivated by Rc-(Rp,Sp)-1,2-dioctylcarbamoylglycero-3-O-p-nitrophenyl octylphosphonate (Rc-trioctyl) with an inactivation half-time of 75 min, while that for the Sc-(Rp,Sp)-1,2-dioctylcarbamoylglycero-3-O-p-nitrophenyl octyl-phosphonate (Sc-trioctyl) compound was 530 min. X-ray structures were obtained of P. cepacia lipase after reaction with Rc-trioctyl to 0.29-nm resolution at pH 4 and covalently modified with Rc-(Rp,Sp)-1,2-dibutylcarbamoylglycero-3-O-p-nitrophenyl butyl-phosphonate (Rc-tributyl) to 0.175-nm resolution at pH 8.5. The three-dimensional structures reveal that both triacylglycerol analogues had reacted with the active-site Ser87, forming a covalent complex. The bound phosphorus atom shows the same chirality (Sp) in both complexes despite the use of a racemic (Rp,Sp) mixture at the phosphorus atom of the triacylglycerol analogues. In the structure of Rc-tributyl-complexed P. cepacia lipase, the diacylglycerol moiety has been lost due to an aging reaction, and only the butyl phosphonate remains visible in the electron density. In the Rc-trioctyl complex the complete inhibitor is clearly defined; it adopts a bent tuning fork conformation. Unambiguously, four binding pockets for the triacylglycerol could be detected: an oxyanion hole and three pockets which accommodate the sn-1, sn-2, and sn-3 fatty acid chains. Van der Waals' interactions are the main forces that keep the radyl groups of the triacylglycerol analogue in position and, in addition, a hydrogen bond to the carbonyl oxygen of the sn-2 chain contributes to fixing the position of the inhibitor.
*[[Lipase 3D Structures|Lipase 3D Structures]]
 
== References ==
==About this Structure==
<references/>
5LIP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LIP OCA].
__TOC__
 
</StructureSection>
==Reference==
Structural basis of the chiral selectivity of Pseudomonas cepacia lipase., Lang DA, Mannesse ML, de Haas GH, Verheij HM, Dijkstra BW, Eur J Biochem. 1998 Jun 1;254(2):333-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9660188 9660188]
[[Category: Burkholderia cepacia]]
[[Category: Burkholderia cepacia]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Triacylglycerol lipase]]
[[Category: Dijkstra BW]]
[[Category: Dijkstra, B W.]]
[[Category: Lang DA]]
[[Category: Lang, D A.]]
[[Category: covalent intermediate]]
[[Category: enantioselectivity]]
[[Category: lipase]]
[[Category: pseudomonadaceae]]
[[Category: triglyceride analogue]]
 
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