In this section
@article{Freemont:2018:10.1016/j.str.2017.12.005,
author = {Freemont, PS and Salih, O and He, S and Planamente, S and Stach, L and MacDonald, J and Manoli, E and Scheres, S and Filloux, A},
doi = {10.1016/j.str.2017.12.005},
journal = {Structure},
pages = {329--336.e3},
title = {Atomic Structure of Type VI Contractile Sheath from Pseudomonas aeruginosa},
url = {http://dx.doi.org/10.1016/j.str.2017.12.005},
volume = {26},
year = {2018}
}
TY - JOUR
AB - Pseudomonas aeruginosa has three type VI secretion systems (T6SSs), H1-, H2-, and H3-T6SS, each belonging to a distinct group. The two T6SS components, TssB/VipA and TssC/VipB, assemble to form tubules that conserve structural/functional homology with tail sheaths of contractile bacteriophages and pyocins. Here, we used cryoelectron microscopy to solve the structure of the H1-T6SS P. aeruginosa TssB1C1 sheath at 3.3 Å resolution. Our structure allowed us to resolve some features of the T6SS sheath that were not resolved in the Vibrio cholerae VipAB and Francisella tularensis IglAB structures. Comparison with sheath structures from other contractile machines, including T4 phage and R-type pyocins, provides a better understanding of how these systems have conserved similar functions/mechanisms despite evolution. We used the P. aeruginosa R2 pyocin as a structural template to build an atomic model of the TssB1C1 sheath in its extended conformation, allowing us to propose a coiled-spring-like mechanism for T6SS sheath contraction.
AU - Freemont,PS
AU - Salih,O
AU - He,S
AU - Planamente,S
AU - Stach,L
AU - MacDonald,J
AU - Manoli,E
AU - Scheres,S
AU - Filloux,A
DO - 10.1016/j.str.2017.12.005
EP - 336
PY - 2018///
SN - 0969-2126
SP - 329
TI - Atomic Structure of Type VI Contractile Sheath from Pseudomonas aeruginosa
T2 - Structure
UR - http://dx.doi.org/10.1016/j.str.2017.12.005
UR - http://hdl.handle.net/10044/1/56130
VL - 26
ER -
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