Format

Send to:

Choose Destination
See comment in PubMed Commons below
Nature. 1993 Apr 29;362(6423):814-20.

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

Author information

  • 1LCCMB-CNRS, Faculté de Médecine Nord, Marseilles, France.

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).

PMID:
8479519
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Nature Publishing Group
    Loading ...
    Write to the Help Desk