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1tgl
From Proteopedia
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| , 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
Page seeded by OCA on Sun Mar 30 23:55:45 2008
