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Research

Biological systems - including the simplest cells - exhibit a broad range of functions to thrive in their environment. Research in the Imperial College Centre for Synthetic Biology is focused on the possibility of engineering the underlying biochemical processes to solve many of the challenges facing society, from healthcare to sustainable energy. In particular, we model, analyse, design and build biological and biochemical systems in living cells and/or in cell extracts, both exploring and enhancing the engineering potential of biology.

As part of our research we develop novel methods to accelerate the celebrated Design-Build-Test-Learn synthetic biology cycle. As such research in the Centre for Synthetic Biology highly multi- and interdisciplinary covering computational modelling and machine learning approaches; automated platform development and genetic circuit engineering ; multi-cellular and multi-organismal interactions, including gene drive and genome engineering; metabolic engineering; in vitro/cell-free synthetic biology; engineered phages and directed evolution; and biomimetics, biomaterials and biological engineering.

Publications

Citation

BibTex format

@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}
}

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RIS format (EndNote, RefMan)

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  -