1i78
From Proteopedia
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CRYSTAL STRUCTURE OF OUTER MEMBRANE PROTEASE OMPT FROM ESCHERICHIA COLI
Overview
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)
About this Structure
1I78 is a Single protein structure of sequence from Escherichia coli with BOG and MPD as ligands. Active as Omptin, with EC number 3.4.23.49 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Nov 20 17:07:07 2007
