1TGL

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

Summary for 1TGL

• Entry DOI: 10.2210/pdb1tgl/pdb
• Descriptor: TRIACYL-GLYCEROL ACYLHYDROLASE (1 entity in total)
• Functional Keywords: hydrolase, carboxylic esterase
• Biological source: Rhizomucor miehei (Mucor miehei)
• Total number of polymer chains: 1
• Total formula weight: 29508.94

Authors

Brady, L.,Brzozowski, A.M.,Derewenda, Z.S.,Dodson, E.J.,Dodson, G.G.,Tolley, S.P.,Turkenburg, J.P.,Christiansen, L.,Huge-Jensen, B.,Norskov, L.,Thim, L. (deposition date: 1990-02-05, release date: 1990-10-15, Last modification date: 2024-02-14)

Primary citation

Brady, L.,Brzozowski, A.M.,Derewenda, Z.S.,Dodson, E.,Dodson, G.,Tolley, S.,Turkenburg, J.P.,Christiansen, L.,Huge-Jensen, B.,Norskov, L.,Thim, L.,Menge, U.
A serine protease triad forms the catalytic centre of a triacylglycerol lipase.
Nature, 343:767-770, 1990

PubMed Abstract: 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.

PubMed: 2304552
DOI: 10.1038/343767a0

Experimental method

X-RAY DIFFRACTION (1.9 Å)