Structure of the T4 baseplate and its function in triggering sheath contraction

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

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Structure of the T4 baseplate and its function in triggering sheath contraction. / Taylor, Nicholas M I; Prokhorov, Nikolai S; Guerrero-Ferreira, Ricardo C; Shneider, Mikhail M; Browning, Christopher; Goldie, Kenneth N; Stahlberg, Henning; Leiman, Petr G.

In: Nature, Vol. 533, No. 7603, 2016, p. 346-352.

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

Harvard

Taylor, NMI, Prokhorov, NS, Guerrero-Ferreira, RC, Shneider, MM, Browning, C, Goldie, KN, Stahlberg, H & Leiman, PG 2016, 'Structure of the T4 baseplate and its function in triggering sheath contraction', Nature, vol. 533, no. 7603, pp. 346-352. https://doi.org/10.1038/nature17971

APA

Taylor, N. M. I., Prokhorov, N. S., Guerrero-Ferreira, R. C., Shneider, M. M., Browning, C., Goldie, K. N., Stahlberg, H., & Leiman, P. G. (2016). Structure of the T4 baseplate and its function in triggering sheath contraction. Nature, 533(7603), 346-352. https://doi.org/10.1038/nature17971

Vancouver

Taylor NMI, Prokhorov NS, Guerrero-Ferreira RC, Shneider MM, Browning C, Goldie KN et al. Structure of the T4 baseplate and its function in triggering sheath contraction. Nature. 2016;533(7603):346-352. https://doi.org/10.1038/nature17971

Author

Taylor, Nicholas M I ; Prokhorov, Nikolai S ; Guerrero-Ferreira, Ricardo C ; Shneider, Mikhail M ; Browning, Christopher ; Goldie, Kenneth N ; Stahlberg, Henning ; Leiman, Petr G. / Structure of the T4 baseplate and its function in triggering sheath contraction. In: Nature. 2016 ; Vol. 533, No. 7603. pp. 346-352.

Bibtex

@article{6609d622e34341b6b5045b13e7b73051,
title = "Structure of the T4 baseplate and its function in triggering sheath contraction",
abstract = "Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This macromolecular machine resembles a stretched, coiled spring (or sheath) wound around a rigid tube with a spike-shaped protein at its tip. A baseplate structure, which is arguably the most complex part of this assembly, relays the contraction signal to the sheath. Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail. We establish the identity and function of a minimal set of components that is conserved in all contractile injection systems and show that the triggering mechanism is universally conserved.",
keywords = "Bacteriophage T4/chemistry, Cryoelectron Microscopy, Crystallography, X-Ray, Models, Molecular, Protein Conformation, Viral Structural Proteins/chemistry",
author = "Taylor, {Nicholas M I} and Prokhorov, {Nikolai S} and Guerrero-Ferreira, {Ricardo C} and Shneider, {Mikhail M} and Christopher Browning and Goldie, {Kenneth N} and Henning Stahlberg and Leiman, {Petr G}",
year = "2016",
doi = "10.1038/nature17971",
language = "English",
volume = "533",
pages = "346--352",
journal = "Nature",
issn = "0028-0836",
publisher = "nature publishing group",
number = "7603",

}

RIS

TY - JOUR

T1 - Structure of the T4 baseplate and its function in triggering sheath contraction

AU - Taylor, Nicholas M I

AU - Prokhorov, Nikolai S

AU - Guerrero-Ferreira, Ricardo C

AU - Shneider, Mikhail M

AU - Browning, Christopher

AU - Goldie, Kenneth N

AU - Stahlberg, Henning

AU - Leiman, Petr G

PY - 2016

Y1 - 2016

N2 - Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This macromolecular machine resembles a stretched, coiled spring (or sheath) wound around a rigid tube with a spike-shaped protein at its tip. A baseplate structure, which is arguably the most complex part of this assembly, relays the contraction signal to the sheath. Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail. We establish the identity and function of a minimal set of components that is conserved in all contractile injection systems and show that the triggering mechanism is universally conserved.

AB - Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This macromolecular machine resembles a stretched, coiled spring (or sheath) wound around a rigid tube with a spike-shaped protein at its tip. A baseplate structure, which is arguably the most complex part of this assembly, relays the contraction signal to the sheath. Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail. We establish the identity and function of a minimal set of components that is conserved in all contractile injection systems and show that the triggering mechanism is universally conserved.

KW - Bacteriophage T4/chemistry

KW - Cryoelectron Microscopy

KW - Crystallography, X-Ray

KW - Models, Molecular

KW - Protein Conformation

KW - Viral Structural Proteins/chemistry

U2 - 10.1038/nature17971

DO - 10.1038/nature17971

M3 - Journal article

C2 - 27193680

VL - 533

SP - 346

EP - 352

JO - Nature

JF - Nature

SN - 0028-0836

IS - 7603

ER -

ID: 194520382