PMID:11566868
| Citation |
Vandeputte-Rutten, L, Kramer, RA, Kroon, J, Dekker, N, Egmond, MR and Gros, P (2001) Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site. EMBO J. 20:5033-9 |
|---|---|
| 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) |
| Links |
PubMed PMC125623 Online version:10.1093/emboj/20.18.5033 |
| Keywords |
Amino Acid Sequence; Aspartic Acid/chemistry; Binding Sites; Catalytic Domain; Crystallography, X-Ray; Escherichia coli/enzymology; Histidine/chemistry; Lipopolysaccharides/metabolism; Models, Molecular; Molecular Sequence Data; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Serine Endopeptidases/chemistry; Serine Endopeptidases/metabolism |
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