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1tgl

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|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]
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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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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tgl OCA], [http://www.ebi.ac.uk/pdbsum/1tgl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tgl RCSB]</span>
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[[Category: hydrolase(carboxylic esterase)]]
[[Category: hydrolase(carboxylic esterase)]]
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Revision as of 20:55, 30 March 2008


PDB ID 1tgl

Drag the structure with the mouse to rotate
, resolution 1.9Å
Activity: Triacylglycerol lipase, with EC number 3.1.1.3
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



A SERINE PROTEASE TRIAD FORMS THE CATALYTIC CENTRE OF A TRIACYLGLYCEROL LIPASE


Overview

True lipases attach triacylglycerols and act at an oil-water interface; they constitute a ubiquitous group of enzymes catalysing a wide variety of reactions, many with industrial potential. But so far the three-dimensional structure has not been reported for any lipase. Here we report the X-ray structure of the Mucor miehei triglyceride lipase and describe the atomic model obtained at 3.1 A resolution and refined to 1.9 A resolution. It reveals a Ser..His..Asp trypsin-like catalytic triad with an active serine buried under a short helical fragment of a long surface loop.

About this Structure

1TGL is a Single protein structure of sequence from Rhizomucor miehei. Full crystallographic information is available from OCA.

Reference

A serine protease triad forms the catalytic centre of a triacylglycerol lipase., Brady L, Brzozowski AM, Derewenda ZS, Dodson E, Dodson G, Tolley S, Turkenburg JP, Christiansen L, Huge-Jensen B, Norskov L, et al., Nature. 1990 Feb 22;343(6260):767-70. PMID:2304552

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