5tgl

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[[Image:5tgl.gif|left|200px]]
[[Image:5tgl.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 5tgl |SIZE=350|CAPTION= <scene name='initialview01'>5tgl</scene>, resolution 3.0&Aring;
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The line below this paragraph, containing "STRUCTURE_5tgl", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=HEE:N-HEXYLPHOSPHONATE+ETHYL+ESTER'>HEE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_5tgl| PDB=5tgl | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tgl OCA], [http://www.ebi.ac.uk/pdbsum/5tgl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=5tgl RCSB]</span>
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}}
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'''A MODEL FOR INTERFACIAL ACTIVATION IN LIPASES FROM THE STRUCTURE OF A FUNGAL LIPASE-INHIBITOR COMPLEX'''
'''A MODEL FOR INTERFACIAL ACTIVATION IN LIPASES FROM THE STRUCTURE OF A FUNGAL LIPASE-INHIBITOR COMPLEX'''
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[[Category: Thim, L.]]
[[Category: Thim, L.]]
[[Category: Turkenburg, J P.]]
[[Category: Turkenburg, J P.]]
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[[Category: hydrolase(carboxylic esterase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:37:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:42:19 2008''
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Revision as of 19:37, 4 May 2008

Image:5tgl.gif

Template:STRUCTURE 5tgl

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 Page seeded by OCA on Sun May 4 22:37:51 2008

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