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1tgl

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(New page: 200px<br /><applet load="1tgl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tgl, resolution 1.9&Aring;" /> '''A SERINE PROTEASE TRI...)
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Revision as of 01:07, 21 November 2007

Image:1tgl.jpg

1tgl, resolution 1.9Å

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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. Active as Triacylglycerol lipase, with EC number 3.1.1.3 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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