Structural characterization of the molecular platform for type III secretion system assembly

Calvin K. Yip, Tyler G. Kimbrough, Heather B. Felise, Marija Vuckovic, Nikhil A. Thomas, Richard A. Pfuetzner, Elizabeth A. Frey, B. Brett Finlay, Samuel I. Miller and Natalie C. J. Strynadka ()
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Calvin K. Yip: University of British Columbia
Tyler G. Kimbrough: University of Washington
Heather B. Felise: Department of Microbiology and Medicine
Marija Vuckovic: University of British Columbia
Nikhil A. Thomas: University of British Columbia
Richard A. Pfuetzner: University of British Columbia
Elizabeth A. Frey: University of British Columbia
B. Brett Finlay: University of British Columbia
Samuel I. Miller: University of Washington
Natalie C. J. Strynadka: University of British Columbia

Nature, 2005, vol. 435, issue 7042, 702-707

Abstract: Abstract Type III secretion systems (TTSSs) are multi-protein macromolecular ‘machines’ that have a central function in the virulence of many Gram-negative pathogens by directly mediating the secretion and translocation of bacterial proteins (termed effectors) into the cytoplasm of eukaryotic cells1. Most of the 20 unique structural components constituting this secretion apparatus are highly conserved among animal and plant pathogens and are also evolutionarily related to proteins in the flagellar-specific export system. Recent electron microscopy experiments have revealed the gross ‘needle-shaped’ morphology of the TTSS2,3,4, yet a detailed understanding of the structural characteristics and organization of these protein components within the bacterial membranes is lacking. Here we report the 1.8-Å crystal structure of EscJ from enteropathogenic Escherichia coli (EPEC), a member of the YscJ/PrgK family whose oligomerization represents one of the earliest events in TTSS assembly5. Crystal packing analysis and molecular modelling indicate that EscJ could form a large 24-subunit ‘ring’ superstructure with extensive grooves, ridges and electrostatic features. Electron microscopy, labelling and mass spectrometry studies on the orthologous Salmonella typhimurium PrgK within the context of the assembled TTSS support the stoichiometry, membrane association and surface accessibility of the modelled ring. We propose that the YscJ/PrgK protein family functions as an essential molecular platform for TTSS assembly.

Date: 2005
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DOI: 10.1038/nature03554

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