The assembly of a GTPase–kinase signalling complex by a bacterial catalytic scaffold

Andrey S. Selyunin, Sarah E. Sutton, Bethany A. Weigele, L. Evan Reddick, Robert C. Orchard, Stefan M. Bresson, Diana R. Tomchick and Neal M. Alto ()
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Andrey S. Selyunin: University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8816, USA
Sarah E. Sutton: University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8816, USA
Bethany A. Weigele: University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8816, USA
L. Evan Reddick: University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8816, USA
Robert C. Orchard: University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8816, USA
Stefan M. Bresson: University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8816, USA
Diana R. Tomchick: University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8816, USA
Neal M. Alto: University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8816, USA

Nature, 2011, vol. 469, issue 7328, 107-111

Abstract: Pathogenic bacteria targets Pathogenic strains of Escherichia coli translocate many proteins into the host cell to promote virulence. The structure of one of these proteins, EspG from E. coli O157:H7, has been determined in a complex with two host enzymes and its mechanism dissected. These structures reveal how EspG disrupts endomembrane trafficking pathways by specifically recognizing the GTP-bound active state of the host's ARF6 enzyme during the vesicle budding reaction at membrane organelles. EspG directly activates PAK kinase by trapping an unfolded transition state in the kinase activation cascade.

Date: 2011
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DOI: 10.1038/nature09593

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