Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography

• Published in: Nature (London) Vol. 362; no. 6423; pp. 814 - 820
• Main Authors: van Tilbeurgh, Herman, Egloff, Marie-Pierre, Martinez, Chrislaine, Rugani, Nathalie, Verger, Robert, Cambillau, Christian
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 29.04.1993; Nature Publishing Group
• Subjects: Analytical, structural and metabolic biochemistry; Binding Sites; Biological and medical sciences; Colipases - chemistry; Computer Simulation; Crystallography; Enzyme Precursors; Enzymes; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Humans; Hydrolases; Lipase - chemistry; Macromolecular Substances; Micelles; Models, Molecular; Oils & fats; Pancreas - enzymology; Phosphatidylcholines - chemistry; Protein Conformation; Protein Precursors - chemistry; Taurodeoxycholic Acid - chemistry; X-Ray Diffraction; X-rays; Enzyme; Active site; Triacylglycerol lipase; Molecular complex; Spatial structure; Induced conformation; Crystalline structure

The three-dimensional structure of the lipase-procolipase complex, co-crystallized with mixed micelles of phosphatidylcholine and bile salt, has been determined at 3 A resolution by X-ray crystallography. The lid, a surface helix covering the catalytic triad of lipase, adopts a totally different con...