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1tgl

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{{STRUCTURE_1tgl| PDB=1tgl | SCENE= }}
{{STRUCTURE_1tgl| PDB=1tgl | SCENE= }}
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'''A SERINE PROTEASE TRIAD FORMS THE CATALYTIC CENTRE OF A TRIACYLGLYCEROL LIPASE'''
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===A SERINE PROTEASE TRIAD FORMS THE CATALYTIC CENTRE OF A TRIACYLGLYCEROL LIPASE===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_2304552}}
==About this Structure==
==About this Structure==
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[[Category: Tolley, S P.]]
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Revision as of 21:43, 28 July 2008

Image:1tgl.png

Template:STRUCTURE 1tgl

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

Template:ABSTRACT PUBMED 2304552

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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