Cryo-EM analysis of the T3S injectisome reveals the structure of the needle and open secretin

J. Hu; L. J. Worrall; C. Hong; M. Vuckovic; C. E. Atkinson; N. Caveney; Z. Yu; N. C. J. Strynadka

doi:10.1038/s41467-018-06298-8

Nature Communications (Sep 2018)

Cryo-EM analysis of the T3S injectisome reveals the structure of the needle and open secretin

J. Hu,
L. J. Worrall,
C. Hong,
M. Vuckovic,
C. E. Atkinson,
N. Caveney,
Z. Yu,
N. C. J. Strynadka

Affiliations

J. Hu: Department of Biochemistry and Molecular Biology and the Centre for Blood Research, University of British Columbia
L. J. Worrall: Department of Biochemistry and Molecular Biology and the Centre for Blood Research, University of British Columbia
C. Hong: CryoEM Shared Resources, Janelia Research Campus, Howard Hughes Medical Institute
M. Vuckovic: Department of Biochemistry and Molecular Biology and the Centre for Blood Research, University of British Columbia
C. E. Atkinson: Department of Biochemistry and Molecular Biology and the Centre for Blood Research, University of British Columbia
N. Caveney: Department of Biochemistry and Molecular Biology and the Centre for Blood Research, University of British Columbia
Z. Yu: CryoEM Shared Resources, Janelia Research Campus, Howard Hughes Medical Institute
N. C. J. Strynadka: Department of Biochemistry and Molecular Biology and the Centre for Blood Research, University of British Columbia

DOI: https://doi.org/10.1038/s41467-018-06298-8
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 11

Abstract

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The bacterial type III secretion system of Gram-negative bacteria uses its core, the needle complex, to penetrate through the infected host cell membrane. Here authors show a near-atomic resolution structure of a needle complex which sheds light on the assembly and function of this nanomachine.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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