Crystal structure of the pilotin from the enterohemorrhagic Escherichia coli type II secretion system.

ABSTRACT: Bacteria contain several sophisticated macromolecular machineries responsible for translocating proteins across the cell envelope. One prominent example is the type II secretion system (T2SS), which contains a large outer membrane channel, called the secretin. These gated channels require specialized proteins, so-called pilotins, to reach and assemble in the outer membrane. Here we report the crystal structure of the pilotin GspS from the T2SS of enterohemorrhagic Escherichia coli (EHEC), an important pathogen that can cause severe disease in cases of food poisoning. In this four-helix protein, the straight helix α2, the curved helix α3 and the bent helix α4 surround the central N-terminal helix α1. The helices of GspS create a prominent groove, mainly formed by side chains of helices α1,

SUBMITTER: Korotkov KV 

PROVIDER: S-EPMC3633704 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature