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Publication Abstract from PubMed

Autotransporters represent a large superfamily of known and putative virulence factors produced by Gram-negative bacteria. They consist of an N-terminal "passenger domain" responsible for the specific effector functions of the molecule and a C-terminal "beta-domain" responsible for translocation of the passenger across the bacterial outer membrane. Here, we present the 2.5-A crystal structure of the passenger domain of the extracellular serine protease EspP, produced by the pathogen Escherichia coli O157:H7 and a member of the serine protease autotransporters of Enterobacteriaceae (SPATEs). Like the previously structurally characterized SPATE passenger domains, the EspP passenger domain contains an extended right-handed parallel beta-helix preceded by an N-terminal globular domain housing the catalytic function of the protease. Of note, however, is the absence of a second globular domain protruding from this beta-helix. We describe the structure of the EspP passenger domain in the context of previous results and provide an alternative hypothesis for the function of the beta-helix within SPATEs.

Crystal Structure of the Passenger Domain of the Escherichia coli Autotransporter EspP.,Khan S, Mian HS, Sandercock LE, Chirgadze NY, Pai EF J Mol Biol. 2011 Sep 22. PMID:21964244^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.