| Title : Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography - van Tilbeurgh_1993_Nature_362_814 |
| Author(s) : van Tilbeurgh H , Egloff MP , Martinez C , Rugani N , Verger R , Cambillau C |
| Ref : Nature , 362 :814 , 1993 |
| 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). |
| ESTHER : van Tilbeurgh_1993_Nature_362_814 |
| PubMedSearch : van Tilbeurgh_1993_Nature_362_814 |
| PubMedID: 8479519 |
| Gene_locus related to this paper: human-PNLIP |
| Gene_locus related to this paper: human-PNLIP |
van Tilbeurgh H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C (1993)
Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography
Nature
362 :814
van Tilbeurgh H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C (1993)
Nature
362 :814