PMID:21964244
| Citation |
Khan, S, Mian, HS, Sandercock, LE, Chirgadze, NY and Pai, EF (2011) Crystal structure of the passenger domain of the Escherichia coli autotransporter EspP. J. Mol. Biol. 413:985-1000 |
|---|---|
| Abstract |
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 "β-domain" responsible for translocation of the passenger across the bacterial outer membrane. Here, we present the 2.5-Å 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 β-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 β-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 β-helix within SPATEs. |
| Links |
PubMed PMC3215816 Online version:10.1016/j.jmb.2011.09.028 |
| Keywords |
Crystallography, X-Ray; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Models, Chemical; Mutagenesis, Site-Directed; Mutation/genetics; Protein Structure, Tertiary; Protein Transport; Serine Endopeptidases/chemistry; Serine Endopeptidases/genetics; Serine Endopeptidases/metabolism |
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