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1eth

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(New page: 200px<br /><applet load="1eth" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eth, resolution 2.8&Aring;" /> '''TRIACYLGLYCEROL LIPAS...)
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[[Image:1eth.gif|left|200px]]<br /><applet load="1eth" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1eth, resolution 2.8&Aring;" />
 
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'''TRIACYLGLYCEROL LIPASE/COLIPASE COMPLEX'''<br />
 
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==Overview==
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==TRIACYLGLYCEROL LIPASE/COLIPASE COMPLEX==
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The crystal structure of the ternary porcine lipase-colipase-tetra, ethylene glycol monooctyl ether (TGME) complex has been determined at 2.8, A resolution. The crystals belong to the cubic space group F23 with a =, 289.1 A and display a strong pseudo-symmetry corresponding to a P23, lattice. Unexpectedly, the crystalline two-domain lipase is found in its, open configuration. This indicates that in the presence of colipase, pure, micelles of the nonionic detergent TGME are able to activate the enzyme; a, process that includes the movement of an N-terminal domain loop (the, flap). The effects of TGME and colipase have been confirmed by chemical, modification of the active site serine residue using diisopropyl, p-nitrophenylphosphate (E600). In addition, the presence of a TGME, molecule tightly bound to the active site pocket shows that TGME acts as a, substrate analog, thus possibly explaining the inhibitory effect of this, nonionic detergent on emulsified substrate hydrolysis at submicellar, concentrations. A comparison of the lipase-colipase interactions between, our porcine complex and the human-porcine complex (van Tilbeurgh, H., Egloff, M.-P., Martinez, C., Rugani, N., Verger, R., and Cambillau, C.(1993) Nature 362, 814-820) indicates that except for one salt bridge, interaction, they are conserved. Analysis of the superimposed complexes, shows a 5.4 degrees rotation on the relative position of the N-terminal, domains excepting the flap that moves in a concerted fashion with the, C-terminal domain. This flexibility may be important for the binding of, the complex to the water-lipid interface.
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<StructureSection load='1eth' size='340' side='right'caption='[[1eth]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1eth]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ETH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ETH 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]] 2.8&#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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1eth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eth OCA], [https://pdbe.org/1eth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eth RCSB], [https://www.ebi.ac.uk/pdbsum/1eth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eth ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LIPP_PIG LIPP_PIG]
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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/et/1eth_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=1eth ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1ETH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with CA, C8E and BME 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=1ETH OCA].
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Lipase activation by nonionic detergents. The crystal structure of the porcine lipase-colipase-tetraethylene glycol monooctyl ether complex., Hermoso J, Pignol D, Kerfelec B, Crenon I, Chapus C, Fontecilla-Camps JC, J Biol Chem. 1996 Jul 26;271(30):18007-16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8663362 8663362]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Triacylglycerol lipase]]
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[[Category: Chapus C]]
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[[Category: Chapus, C.]]
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[[Category: Crenon I]]
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[[Category: Crenon, I.]]
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[[Category: Fontecilla-Camps JC]]
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[[Category: Fontecilla-Camps, J.C.]]
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[[Category: Hermoso J]]
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[[Category: Hermoso, J.]]
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[[Category: Kerfelec B]]
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[[Category: Kerfelec, B.]]
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[[Category: Pignol D]]
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[[Category: Pignol, D.]]
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[[Category: BME]]
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[[Category: C8E]]
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[[Category: CA]]
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[[Category: complex (hydrolase/cofactor)]]
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[[Category: lipid degradation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:18:00 2007''
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Current revision

TRIACYLGLYCEROL LIPASE/COLIPASE COMPLEX

PDB ID 1eth

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