5tgl
From Proteopedia
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| - | [[Image:5tgl.gif|left|200px]] | + | [[Image:5tgl.gif|left|200px]] |
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| - | '''A MODEL FOR INTERFACIAL ACTIVATION IN LIPASES FROM THE STRUCTURE OF A FUNGAL LIPASE-INHIBITOR COMPLEX''' | + | {{Structure |
| + | |PDB= 5tgl |SIZE=350|CAPTION= <scene name='initialview01'>5tgl</scene>, resolution 3.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HEE:N-HEXYLPHOSPHONATE ETHYL ESTER'>HEE</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= | ||
| + | }} | ||
| + | |||
| + | '''A MODEL FOR INTERFACIAL ACTIVATION IN LIPASES FROM THE STRUCTURE OF A FUNGAL LIPASE-INHIBITOR COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 5TGL is a [ | + | 5TGL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhizomucor_miehei Rhizomucor miehei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TGL OCA]. |
==Reference== | ==Reference== | ||
| - | A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex., Brzozowski AM, Derewenda U, Derewenda ZS, Dodson GG, Lawson DM, Turkenburg JP, Bjorkling F, Huge-Jensen B, Patkar SA, Thim L, Nature. 1991 Jun 6;351(6326):491-4. PMID:[http:// | + | A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex., Brzozowski AM, Derewenda U, Derewenda ZS, Dodson GG, Lawson DM, Turkenburg JP, Bjorkling F, Huge-Jensen B, Patkar SA, Thim L, Nature. 1991 Jun 6;351(6326):491-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2046751 2046751] |
[[Category: Rhizomucor miehei]] | [[Category: Rhizomucor miehei]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase(carboxylic esterase)]] | [[Category: hydrolase(carboxylic esterase)]] | ||
| - | ''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 19:12:57 2008'' |
Revision as of 17:12, 20 March 2008
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| , resolution 3.0Å | |||||||
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| Ligands: | |||||||
| Activity: | Triacylglycerol lipase, with EC number 3.1.1.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
A MODEL FOR INTERFACIAL ACTIVATION IN LIPASES FROM THE STRUCTURE OF A FUNGAL LIPASE-INHIBITOR COMPLEX
Overview
Lipases are hydrolytic enzymes which break down triacylglycerides into free fatty acids and glycerols. They have been classified as serine hydrolases owing to their inhibition by diethyl p-nitrophenyl phosphate. Lipase activity is greatly increased at the lipid-water interface, a phenomenon known as interfacial activation. X-ray analysis has revealed the atomic structures of two triacylglycerol lipases, unrelated in sequence: the human pancreatic lipase (hPL)4, and an enzyme isolated from the fungus Rhizomucor (formerly Mucor) miehei (RmL). In both enzymes the active centres contain structurally analogous Asp-His-Ser triads (characteristic of serine proteinases), which are buried completely beneath a short helical segment, or 'lid'. Here we present the crystal structure (at 3 A resolution) of a complex of R. miehei lipase with n-hexylphosphonate ethyl ester in which the enzyme's active site is exposed by the movement of the helical lid. This movement also increases the nonpolarity of the surface surrounding the catalytic site. We propose that the structure of the enzyme in this complex is equivalent to the activated state generated by the oil-water interface.
About this Structure
5TGL is a Single protein structure of sequence from Rhizomucor miehei. Full crystallographic information is available from OCA.
Reference
A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex., Brzozowski AM, Derewenda U, Derewenda ZS, Dodson GG, Lawson DM, Turkenburg JP, Bjorkling F, Huge-Jensen B, Patkar SA, Thim L, Nature. 1991 Jun 6;351(6326):491-4. PMID:2046751
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