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