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Topology and organization of the Salmonella typhimurium type III secretion needle complex components.

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Topology and organization of the Salmonella typhimurium type III secretion needle complex components. / Schraidt, Oliver; Lefebre, Matthew D; Brunner, Matthias J; Schmied, Wolfgang H; Schmidt, Andreas; Radics, Julia; Mechtler, Karl; Galán, Jorge E; Marlovits, Thomas.

In: PLOS PATHOG, Vol. 6, No. 4, 4, 2010, p. 1000824.

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

Harvard

Schraidt, O, Lefebre, MD, Brunner, MJ, Schmied, WH, Schmidt, A, Radics, J, Mechtler, K, Galán, JE & Marlovits, T 2010, 'Topology and organization of the Salmonella typhimurium type III secretion needle complex components.', PLOS PATHOG, vol. 6, no. 4, 4, pp. 1000824. https://doi.org/10.1371/journal.ppat.1000824

APA

Schraidt, O., Lefebre, M. D., Brunner, M. J., Schmied, W. H., Schmidt, A., Radics, J., Mechtler, K., Galán, J. E., & Marlovits, T. (2010). Topology and organization of the Salmonella typhimurium type III secretion needle complex components. PLOS PATHOG, 6(4), 1000824. [4]. https://doi.org/10.1371/journal.ppat.1000824

Vancouver

Schraidt O, Lefebre MD, Brunner MJ, Schmied WH, Schmidt A, Radics J et al. Topology and organization of the Salmonella typhimurium type III secretion needle complex components. PLOS PATHOG. 2010;6(4):1000824. 4. https://doi.org/10.1371/journal.ppat.1000824

Bibtex

@article{075af374d19543b3b6a4ccafb03f058f,
title = "Topology and organization of the Salmonella typhimurium type III secretion needle complex components.",
abstract = "The correct organization of single subunits of multi-protein machines in a three dimensional context is critical for their functionality. Type III secretion systems (T3SS) are molecular machines with the capacity to deliver bacterial effector proteins into host cells and are fundamental for the biology of many pathogenic or symbiotic bacteria. A central component of T3SSs is the needle complex, a multiprotein structure that mediates the passage of effector proteins through the bacterial envelope. We have used cryo electron microscopy combined with bacterial genetics, site-specific labeling, mutational analysis, chemical derivatization and high-resolution mass spectrometry to generate an experimentally validated topographic map of a Salmonella typhimurium T3SS needle complex. This study provides insights into the organization of this evolutionary highly conserved nanomachinery and is the basis for further functional analysis.",
keywords = "Macromolecular Substances, Cryoelectron Microscopy, Bacterial Proteins/*chemistry/*ultrastructure, Membrane Transport Proteins/*chemistry/*ultrastructure, Salmonella typhimurium/*chemistry/*ultrastructure, Macromolecular Substances, Cryoelectron Microscopy, Bacterial Proteins/*chemistry/*ultrastructure, Membrane Transport Proteins/*chemistry/*ultrastructure, Salmonella typhimurium/*chemistry/*ultrastructure",
author = "Oliver Schraidt and Lefebre, {Matthew D} and Brunner, {Matthias J} and Schmied, {Wolfgang H} and Andreas Schmidt and Julia Radics and Karl Mechtler and Gal{\'a}n, {Jorge E} and Thomas Marlovits",
year = "2010",
doi = "10.1371/journal.ppat.1000824",
language = "English",
volume = "6",
pages = "1000824",
journal = "PLOS PATHOG",
issn = "1553-7366",
publisher = "Public Library of Science",
number = "4",

}

RIS

TY - JOUR

T1 - Topology and organization of the Salmonella typhimurium type III secretion needle complex components.

AU - Schraidt, Oliver

AU - Lefebre, Matthew D

AU - Brunner, Matthias J

AU - Schmied, Wolfgang H

AU - Schmidt, Andreas

AU - Radics, Julia

AU - Mechtler, Karl

AU - Galán, Jorge E

AU - Marlovits, Thomas

PY - 2010

Y1 - 2010

N2 - The correct organization of single subunits of multi-protein machines in a three dimensional context is critical for their functionality. Type III secretion systems (T3SS) are molecular machines with the capacity to deliver bacterial effector proteins into host cells and are fundamental for the biology of many pathogenic or symbiotic bacteria. A central component of T3SSs is the needle complex, a multiprotein structure that mediates the passage of effector proteins through the bacterial envelope. We have used cryo electron microscopy combined with bacterial genetics, site-specific labeling, mutational analysis, chemical derivatization and high-resolution mass spectrometry to generate an experimentally validated topographic map of a Salmonella typhimurium T3SS needle complex. This study provides insights into the organization of this evolutionary highly conserved nanomachinery and is the basis for further functional analysis.

AB - The correct organization of single subunits of multi-protein machines in a three dimensional context is critical for their functionality. Type III secretion systems (T3SS) are molecular machines with the capacity to deliver bacterial effector proteins into host cells and are fundamental for the biology of many pathogenic or symbiotic bacteria. A central component of T3SSs is the needle complex, a multiprotein structure that mediates the passage of effector proteins through the bacterial envelope. We have used cryo electron microscopy combined with bacterial genetics, site-specific labeling, mutational analysis, chemical derivatization and high-resolution mass spectrometry to generate an experimentally validated topographic map of a Salmonella typhimurium T3SS needle complex. This study provides insights into the organization of this evolutionary highly conserved nanomachinery and is the basis for further functional analysis.

KW - Macromolecular Substances

KW - Cryoelectron Microscopy

KW - Bacterial Proteins/chemistry/ultrastructure

KW - Membrane Transport Proteins/chemistry/ultrastructure

KW - Salmonella typhimurium/chemistry/ultrastructure

KW - Macromolecular Substances

KW - Cryoelectron Microscopy

KW - Bacterial Proteins/chemistry/ultrastructure

KW - Membrane Transport Proteins/chemistry/ultrastructure

KW - Salmonella typhimurium/chemistry/ultrastructure

U2 - 10.1371/journal.ppat.1000824

DO - 10.1371/journal.ppat.1000824

M3 - SCORING: Journal article

VL - 6

SP - 1000824

JO - PLOS PATHOG

JF - PLOS PATHOG

SN - 1553-7366

IS - 4

M1 - 4

ER -