Research ExplorerPublicationsThe Structure of the Type III Secretion System Needle Comple...

The Structure of the Type III Secretion System Needle Complex

Standard

The Structure of the Type III Secretion System Needle Complex. / Miletic, Sean; Goessweiner-Mohr, Nikolaus; Marlovits, Thomas C.

In: CURR TOP MICROBIOL, 31.10.2019.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Miletic, S, Goessweiner-Mohr, N & Marlovits, TC 2019, 'The Structure of the Type III Secretion System Needle Complex', CURR TOP MICROBIOL. https://doi.org/10.1007/82_2019_178

APA

Miletic, S., Goessweiner-Mohr, N., & Marlovits, T. C. (2019). The Structure of the Type III Secretion System Needle Complex. CURR TOP MICROBIOL. https://doi.org/10.1007/82_2019_178

Vancouver

Miletic S, Goessweiner-Mohr N, Marlovits TC. The Structure of the Type III Secretion System Needle Complex. CURR TOP MICROBIOL. 2019 Oct 31. https://doi.org/10.1007/82_2019_178

Bibtex

@article{a2c829d2248b4ce6b9346b3508fe7e88,
title = "The Structure of the Type III Secretion System Needle Complex",
abstract = "The type III secretion system (T3SS) is an essential virulence factor of many pathogenic bacterial species including Salmonella, Yersinia, Shigella and enteropathogenic Escherichia coli (EPEC). It is an intricate molecular machine that spans the bacterial membranes and injects effector proteins into target host cells, enabling bacterial infection. The T3SS needle complex comprises of proteinaceous rings supporting a needle filament which extends out into the extracellular environment. It serves as the central conduit for translocating effector proteins. Multiple laboratories have dedicated a remarkable effort to decipher the structure and function of the needle complex. A combination of structural biology techniques such as cryo-electron microscopy (cryoEM), X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy and computer modelling have been utilized to study different structural components at progressively higher resolutions. This chapter will provide an overview of the structural details of the T3SS needle complex, shedding light on this essential component of this fascinating bacterial system.",
author = "Sean Miletic and Nikolaus Goessweiner-Mohr and Marlovits, {Thomas C}",
year = "2019",
month = oct,
day = "31",
doi = "10.1007/82_2019_178",
language = "English",
journal = "CURR TOP MICROBIOL",
issn = "0070-217X",
publisher = "Springer",

}

RIS

TY - JOUR

T1 - The Structure of the Type III Secretion System Needle Complex

AU - Miletic, Sean

AU - Goessweiner-Mohr, Nikolaus

AU - Marlovits, Thomas C

PY - 2019/10/31

Y1 - 2019/10/31

N2 - The type III secretion system (T3SS) is an essential virulence factor of many pathogenic bacterial species including Salmonella, Yersinia, Shigella and enteropathogenic Escherichia coli (EPEC). It is an intricate molecular machine that spans the bacterial membranes and injects effector proteins into target host cells, enabling bacterial infection. The T3SS needle complex comprises of proteinaceous rings supporting a needle filament which extends out into the extracellular environment. It serves as the central conduit for translocating effector proteins. Multiple laboratories have dedicated a remarkable effort to decipher the structure and function of the needle complex. A combination of structural biology techniques such as cryo-electron microscopy (cryoEM), X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy and computer modelling have been utilized to study different structural components at progressively higher resolutions. This chapter will provide an overview of the structural details of the T3SS needle complex, shedding light on this essential component of this fascinating bacterial system.

AB - The type III secretion system (T3SS) is an essential virulence factor of many pathogenic bacterial species including Salmonella, Yersinia, Shigella and enteropathogenic Escherichia coli (EPEC). It is an intricate molecular machine that spans the bacterial membranes and injects effector proteins into target host cells, enabling bacterial infection. The T3SS needle complex comprises of proteinaceous rings supporting a needle filament which extends out into the extracellular environment. It serves as the central conduit for translocating effector proteins. Multiple laboratories have dedicated a remarkable effort to decipher the structure and function of the needle complex. A combination of structural biology techniques such as cryo-electron microscopy (cryoEM), X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy and computer modelling have been utilized to study different structural components at progressively higher resolutions. This chapter will provide an overview of the structural details of the T3SS needle complex, shedding light on this essential component of this fascinating bacterial system.

U2 - 10.1007/82_2019_178

DO - 10.1007/82_2019_178

M3 - SCORING: Journal article

C2 - 31667599

JO - CURR TOP MICROBIOL

JF - CURR TOP MICROBIOL

SN - 0070-217X

ER -