Ontology highlight
ABSTRACT:
SUBMITTER: Vandeputte-Rutten L
PROVIDER: S-EPMC125623 | biostudies-literature | 2001 Sep
REPOSITORIES: biostudies-literature
The EMBO journal 20010901 18
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 ...[more]