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| - | [[Image:1eth.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1eth| PDB=1eth | SCENE= }} | | {{STRUCTURE_1eth| PDB=1eth | SCENE= }} |
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| - | '''TRIACYLGLYCEROL LIPASE/COLIPASE COMPLEX'''
| + | ===TRIACYLGLYCEROL LIPASE/COLIPASE COMPLEX=== |
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| - | ==Overview==
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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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8663362}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8663362 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8663362}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Pignol, D.]] | | [[Category: Pignol, D.]] |
| | [[Category: Lipid degradation]] | | [[Category: Lipid degradation]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:30:01 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:57:14 2008'' |
Revision as of 22:57, 30 June 2008
Template:STRUCTURE 1eth
TRIACYLGLYCEROL LIPASE/COLIPASE COMPLEX
Template:ABSTRACT PUBMED 8663362
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 Tue Jul 1 01:57:14 2008
