Crystal structure of the passenger domain of the Escherichia coli autotransporter EspP.

Autor: Khan S; Campbell Family Cancer Research Institute, Ontario Cancer Institute, University Health Network, Toronto Medical Discovery Tower, Toronto, Ontario, Canada M5G 1L7., Mian HS, Sandercock LE, Chirgadze NY, Pai EF
Jazyk: angličtina
Zdroj: Journal of molecular biology [J Mol Biol] 2011 Nov 11; Vol. 413 (5), pp. 985-1000. Date of Electronic Publication: 2011 Sep 22.
DOI: 10.1016/j.jmb.2011.09.028
Abstrakt: 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.
(Copyright © 2011 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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