1LPA
INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY
Summary for 1LPA
| Entry DOI | 10.2210/pdb1lpa/pdb |
| Descriptor | COLIPASE, LIPASE, nonyl beta-D-glucopyranoside, ... (5 entities in total) |
| Functional Keywords | hydrolase(carboxylic esterase) |
| Biological source | Sus scrofa (pig) More |
| Cellular location | Secreted: P02703 P16233 |
| Total number of polymer chains | 2 |
| Total formula weight | 60888.60 |
| Authors | Van Tilbeurgh, H.,Egloff, M.-P.,Cambillau, C. (deposition date: 1994-08-19, release date: 1994-11-01, Last modification date: 2024-11-06) |
| Primary citation | van Tilbeurgh, H.,Egloff, M.P.,Martinez, C.,Rugani, N.,Verger, R.,Cambillau, C. Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature, 362:814-820, 1993 Cited by PubMed Abstract: 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 conformation which allows phospholipid to bind to the enzyme's active site. The open lid is an essential component of the active site and interacts with procolipase. Together they form the lipid-water interface binding site. This reorganization of the lid structure provokes a second drastic conformational change in an active site loop, which in its turn creates the oxyanion hole (induced fit). PubMed: 8479519DOI: 10.1038/362814a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.04 Å) |
Structure validation
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