1eth
From Proteopedia
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| - | [[Image:1eth.gif|left|200px]] | + | [[Image:1eth.gif|left|200px]] |
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| - | '''TRIACYLGLYCEROL LIPASE/COLIPASE COMPLEX''' | + | {{Structure |
| + | |PDB= 1eth |SIZE=350|CAPTION= <scene name='initialview01'>1eth</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''TRIACYLGLYCEROL LIPASE/COLIPASE COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ETH is a [ | + | 1ETH is a [[Protein complex]] structure of sequences from [http://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]. |
==Reference== | ==Reference== | ||
| - | 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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/8663362 8663362] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: lipid degradation]] | [[Category: lipid degradation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:00:06 2008'' |
Revision as of 09:00, 20 March 2008
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Triacylglycerol lipase, with EC number 3.1.1.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TRIACYLGLYCEROL LIPASE/COLIPASE COMPLEX
Overview
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.
About this Structure
1ETH is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.
Reference
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:8663362
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