Journal Article

PUBDB-2024-00591

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Cryo-EM structure of the Shigella type III needle complex

Lunelli, M. ; Kamprad, A.Extern* ; Bürger, J. ; Mielke, T. ; Spahn, C. M. T. ; Kolbe, M. (Corresponding author)CSSB*

2020
PLoS Lawrence, Kan.

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Please use a persistent id in citations: doi:10.1371/journal.ppat.1008263  doi:10.3204/PUBDB-2024-00591

Abstract: The Type III Secretion Systems (T3SS) needle complex is a conserved syringe-shaped protein translocation nanomachine with a mass of about 3.5 MDa essential for the survival and virulence of many Gram-negative bacterial pathogens. This system is composed of a membrane-embedded basal body and an extracellular needle that deliver effector proteins into host cells. High-resolution structures of the T3SS from different organisms and infection stages are needed to understand the underlying molecular mechanisms of effector translocation. Here, we present the cryo-electron microscopy structure of the isolated Shigella T3SS needle complex. The inner membrane (IM) region of the basal body adopts 24-fold rotational symmetry and forms a channel system that connects the bacterial periplasm with the export apparatus cage. The secretin oligomer adopts a heterogeneous architecture with 16- and 15-fold cyclic symmetry in the periplasmic N-terminal connector and C-terminal outer membrane ring, respectively. Two out of three IM subunits bind the secretin connector via a β-sheet augmentation. The cryo-EM map also reveals the helical architecture of the export apparatus core, the inner rod, the needle and their intervening interfaces.

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Contributing Institute(s):

1. CSSB-HZI-MK (CSSB-HZI-MK)

Research Program(s):

1. 899 - ohne Topic (POF4-899) (POF4-899)
2. iNEXT - Infrastructure for NMR, EM and X-rays for translational research (653706) (653706)
3. FUTURE T3SS - Bacterial effector secretion: Function and Architecture of the Type 3 Secretion System (311374) (311374)

Experiment(s):

1. No specific instrument

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