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Type III secretion systems shape up as they ship out.

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Type III secretion systems shape up as they ship out. / Marlovits, Thomas; Stebbins, C Erec.

In: CURR OPIN MICROBIOL, Vol. 13, No. 1, 1, 2010, p. 47-52.

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

Harvard

Marlovits, T & Stebbins, CE 2010, 'Type III secretion systems shape up as they ship out.', CURR OPIN MICROBIOL, vol. 13, no. 1, 1, pp. 47-52. <http://www.ncbi.nlm.nih.gov/pubmed/20015680?dopt=Citation>

APA

Marlovits, T., & Stebbins, C. E. (2010). Type III secretion systems shape up as they ship out. CURR OPIN MICROBIOL, 13(1), 47-52. [1]. http://www.ncbi.nlm.nih.gov/pubmed/20015680?dopt=Citation

Vancouver

Marlovits T, Stebbins CE. Type III secretion systems shape up as they ship out. CURR OPIN MICROBIOL. 2010;13(1):47-52. 1.

Bibtex

@article{e4fac82371f640fdb5773ba10879cbbf,
title = "Type III secretion systems shape up as they ship out.",
abstract = "Virulence associated protein type III secretion systems (T3SSs) are intricately structured organic nanosyringes that achieve the translocation of bacterial proteins from the prokaryotic cytoplasm across three membranes into the host cytosol. The substrates for these systems number in the hundreds, with remarkably diverse biological activities, modulating host cell biology for the benefit of the pathogen. Although there has been tremendous progress on the structure and function of the T3SS substrates, there has been comparatively little progress on the much more highly conserved secretion apparatus itself. This review summarizes recent advances in the field of structural microbiology that have begun to address this shortcoming, finally bringing to bear the power of structural biology to this central virulence system of Gram-negative bacterial pathogens.",
keywords = "Models, Biological, Protein Binding, Bacterial Proteins/chemistry/*metabolism/ultrastructure, Macromolecular Substances/chemistry/*metabolism, Membrane Transport Proteins/chemistry/*metabolism/ultrastructure, Models, Chemical, *Protein Folding, Virulence Factors/metabolism, Models, Biological, Protein Binding, Bacterial Proteins/chemistry/*metabolism/ultrastructure, Macromolecular Substances/chemistry/*metabolism, Membrane Transport Proteins/chemistry/*metabolism/ultrastructure, Models, Chemical, *Protein Folding, Virulence Factors/metabolism",
author = "Thomas Marlovits and Stebbins, {C Erec}",
year = "2010",
language = "English",
volume = "13",
pages = "47--52",
number = "1",

}

RIS

TY - JOUR

T1 - Type III secretion systems shape up as they ship out.

AU - Marlovits, Thomas

AU - Stebbins, C Erec

PY - 2010

Y1 - 2010

N2 - Virulence associated protein type III secretion systems (T3SSs) are intricately structured organic nanosyringes that achieve the translocation of bacterial proteins from the prokaryotic cytoplasm across three membranes into the host cytosol. The substrates for these systems number in the hundreds, with remarkably diverse biological activities, modulating host cell biology for the benefit of the pathogen. Although there has been tremendous progress on the structure and function of the T3SS substrates, there has been comparatively little progress on the much more highly conserved secretion apparatus itself. This review summarizes recent advances in the field of structural microbiology that have begun to address this shortcoming, finally bringing to bear the power of structural biology to this central virulence system of Gram-negative bacterial pathogens.

AB - Virulence associated protein type III secretion systems (T3SSs) are intricately structured organic nanosyringes that achieve the translocation of bacterial proteins from the prokaryotic cytoplasm across three membranes into the host cytosol. The substrates for these systems number in the hundreds, with remarkably diverse biological activities, modulating host cell biology for the benefit of the pathogen. Although there has been tremendous progress on the structure and function of the T3SS substrates, there has been comparatively little progress on the much more highly conserved secretion apparatus itself. This review summarizes recent advances in the field of structural microbiology that have begun to address this shortcoming, finally bringing to bear the power of structural biology to this central virulence system of Gram-negative bacterial pathogens.

KW - Models, Biological

KW - Protein Binding

KW - Bacterial Proteins/chemistry/metabolism/ultrastructure

KW - Macromolecular Substances/chemistry/metabolism

KW - Membrane Transport Proteins/chemistry/metabolism/ultrastructure

KW - Models, Chemical

KW - Protein Folding

KW - Virulence Factors/metabolism

KW - Models, Biological

KW - Protein Binding

KW - Bacterial Proteins/chemistry/metabolism/ultrastructure

KW - Macromolecular Substances/chemistry/metabolism

KW - Membrane Transport Proteins/chemistry/metabolism/ultrastructure

KW - Models, Chemical

KW - Protein Folding

KW - Virulence Factors/metabolism

M3 - SCORING: Journal article

VL - 13

SP - 47

EP - 52

IS - 1

M1 - 1

ER -