Structural analysis of the essential self-cleaving type III secretion proteins EscU and SpaS

Raz Zarivach, Wanyin Deng, Marija Vuckovic, Heather B. Felise, Hai V. Nguyen, Samuel I. Miller, B. Brett Finlay and Natalie C. J. Strynadka ()
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Raz Zarivach: and the Center for Blood Research, University of British Columbia, 2350 Health Sciences Mall, Vancouver, British Columbia V6T 1Z3, Canada
Wanyin Deng: Michael Smith Laboratories, University of British Columbia, 2185 East Mall, Vancouver, British Columbia V6T 1Z4, Canada
Marija Vuckovic: and the Center for Blood Research, University of British Columbia, 2350 Health Sciences Mall, Vancouver, British Columbia V6T 1Z3, Canada
Heather B. Felise: HSB K-140, Box 357710, Seattle, Washington 98195, USA
Hai V. Nguyen: HSB K-140, Box 357710, Seattle, Washington 98195, USA
Samuel I. Miller: HSB K-140, Box 357710, Seattle, Washington 98195, USA
B. Brett Finlay: Michael Smith Laboratories, University of British Columbia, 2185 East Mall, Vancouver, British Columbia V6T 1Z4, Canada
Natalie C. J. Strynadka: and the Center for Blood Research, University of British Columbia, 2350 Health Sciences Mall, Vancouver, British Columbia V6T 1Z3, Canada

Nature, 2008, vol. 453, issue 7191, 124-127

Abstract: A type II β-turn in the Escherichia coli protein EscU undergoes auto-cleavage via a mechanism involving cyclization of a conserved asparagine residue. Structural and in vivo analysis of point and deletion mutations illustrates the subtle conformational effects of auto-cleavage in modulating the molecular features of a highly conserved surface region of EscU, a potential point of interaction with other T3SS components at the inner membrane.

Date: 2008
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DOI: 10.1038/nature06832

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