1eth: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1eth.gif|left|200px]] | [[Image:1eth.gif|left|200px]] | ||
'''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== | ||
| Line 7: | Line 16: | ||
==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]] | ||
| Line 26: | Line 35: | ||
[[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
| |||||||||||||
| 1eth, resolution 2.8Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | CA, C8E and BME | ||||||||||||
| 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
Page seeded by OCA on Thu Mar 20 11:00:06 2008