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Atomic Structure of Type VI Contractile Sheath from Pseudomonas aeruginosa

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Title: Atomic Structure of Type VI Contractile Sheath from Pseudomonas aeruginosa
Authors: Freemont, PS
Salih, O
He, S
Planamente, S
Stach, L
MacDonald, J
Manoli, E
Scheres, S
Filloux, A
Item Type: Journal Article
Abstract: 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.
Issue Date: 4-Jan-2018
Date of Acceptance: 6-Dec-2017
URI: http://hdl.handle.net/10044/1/56130
DOI: https://dx.doi.org/10.1016/j.str.2017.12.005
ISSN: 0969-2126
Publisher: Elsevier
Start Page: 329
End Page: 336.e3
Journal / Book Title: Structure
Volume: 26
Issue: 2
Copyright Statement: Creative Commons Attribution 4.0 International (CC BY 4.0)
Sponsor/Funder: Medical Research Council (MRC)
Funder's Grant Number: MR/K001930/1
Keywords: T6SS
helical structure
molecular evolution
06 Biological Sciences
08 Information And Computing Sciences
03 Chemical Sciences
Publication Status: Published
Appears in Collections:Department of Medicine (up to 2019)
Faculty of Natural Sciences