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- Title
Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site.
- Authors
Vandeputte-Rutten, L; Kramer, R A; Kroon, J; Dekker, N; Egmond, M R; Gros, P
- Abstract
OmpT from Escherichia coli belongs to a family of highly homologous outer membrane proteases, known as omptins, which are implicated in the virulence of several pathogenic Gram-negative bacteria. Here we present the crystal structure of OmpT, which shows a 10-stranded antiparallel beta-barrel that protrudes far from the lipid bilayer into the extracellular space. We identified a putative binding site for lipopolysaccharide, a molecule that is essential for OmpT activity. The proteolytic site is located in a groove at the extracellular top of the vase-shaped beta-barrel. Based on the constellation of active site residues, we propose a novel proteolytic mechanism, involving a His-Asp dyad and an Asp-Asp couple that activate a putative nucleophilic water molecule. The active site is fully conserved within the omptin family. Therefore, the structure described here provides a sound basis for the design of drugs against omptin-mediated bacterial pathogenesis. Coordinates are in the Protein Data Bank (accession No. 1I78)
- Publication
The EMBO journal, 2001, Vol 20, Issue 18, p5033
- ISSN
0261-4189
- Publication type
Journal Article
- DOI
10.1093/emboj/20.18.5033