Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site
AUTOR(ES)
Vandeputte-Rutten, Lucy
FONTE
Oxford University Press
RESUMO
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 β-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 β-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)
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=125623Documentos Relacionados
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