1i78

Publication Abstract from PubMed

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)

Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site.,Vandeputte-Rutten L, Kramer RA, Kroon J, Dekker N, Egmond MR, Gros P EMBO J. 2001 Sep 17;20(18):5033-9. PMID:11566868^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.