1I78
CRYSTAL STRUCTURE OF OUTER MEMBRANE PROTEASE OMPT FROM ESCHERICHIA COLI
Summary for 1I78
| Entry DOI | 10.2210/pdb1i78/pdb |
| Descriptor | PROTEASE VII, octyl beta-D-glucopyranoside, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total) |
| Functional Keywords | integral outer membrane protein, protease, beta barrel, hydrolase |
| Biological source | Escherichia coli |
| Cellular location | Cell outer membrane; Multi-pass membrane protein: P09169 |
| Total number of polymer chains | 2 |
| Total formula weight | 68397.01 |
| Authors | Vandeputte-Rutten, L.,Kramer, R.A.,Kroon, J.,Dekker, N.,Egmond, M.R.,Gros, P. (deposition date: 2001-03-08, release date: 2001-10-03, Last modification date: 2024-02-07) |
| Primary citation | Vandeputte-Rutten, L.,Kramer, R.A.,Kroon, J.,Dekker, N.,Egmond, M.R.,Gros, P. Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site. EMBO J., 20:5033-5039, 2001 Cited by PubMed 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) PubMed: 11566868DOI: 10.1093/emboj/20.18.5033 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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