van Tilbeurgh_1993_Nature_362_814

Reference

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).

PubMedSearch : van Tilbeurgh_1993_Nature_362_814
PubMedID: 8479519
Gene_locus related to this paper: human-PNLIP

Related information

Inhibitor MUP
Substrate MUP    Dilauroyl-lecithin
Gene_locus MUP    Dilauroyl-lecithin    human-PNLIP
Structure MUP    Dilauroyl-lecithin    human-PNLIP    1LPA    1LPB

Citations formats

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