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The structure and function of the beta-barrel assembly machinery

Project Description

Anti-microbial resistance is a major threat to human health in the 21st Century, and finding targets against which we can develop new therapies that overcome growing resistance to existing antibiotics is an urgent, unmet need.

In this project we will use state of the art cryo-electron microscopy to generate new insight into the structure and function of a membrane protein complex that is essential for viability and pathogenesis of some the most serious bacterial pathogens. We will use the state-of-the-art Titan Krios microscopes in Leeds to do single-particle cryo-EM, and determine the structure of the E. coli beta-barrel assembly machinery (or “BAM” complex) to atomic resolution. We will also determine the structures of BAM bound to one of a range of natural binding partners that modulate function, and to neutralizing antibodies.

The overall aim is to provide new mechanistic insights into membrane protein biogenesis, discover new routes to novel anti-biotics, and provide training in state-of-the-art structural biology methods.

Funding Notes

White Rose BBSRC Doctoral Training Partnership in Mechanistic Biology
4 year fully-funded programme of integrated research and skills training, starting Oct 2019:
• Research Council Stipend
• UK/EU Tuition Fees
• Conference allowance
• Research Costs

At least a 2:1 honours degree or equivalent. We welcome students with backgrounds in biological, chemical or physical sciences, or mathematical backgrounds with an interest in biological questions.
EU candidates require 3 years of UK residency in order to receive full studentship

Not all projects advertised will be funded; the DTP will appoint a limited number of candidates via a competitive process.

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Patel, N.*, White, S.J.*, Thompson, R.F., Weiß, E.U.1, Bingham, R.1, Zlotnick, A.2, Dykeman, E.1, Twarock, R.,1‡ Ranson, N.A.‡ & Stockley, P.G.‡ (2017). The HBV RNA pregenome encodes specific interactions with the viral core protein that can promote nucleocapsid assembly. Nature Microbiology, DOI:10.1038/nmicrobiol.2017.98

Iadanza, M.G*., Higgins, A.J.*, Schiffrin, R., Calabrese, A., Brockwell, D.J., Ashcroft, A.E. Radford, S.E. ‡ & Ranson, N.A.‡ (2016). Lateral opening of the intact β-barrel assembly machinery captured by cryo-EM Nature Comms. DOI:10.1038/ncomms12865.

Hesketh, E.L., Meshcheriakova, Y., Dent, K.C., Saxena, P., Thompson, R.F., Cockburn, J.J.B, Lomonossoff, G.P. & Ranson, N.A. (2015). Mechanisms of assembly and genome packaging in an RNA virus revealed by high-resolution cryo-EM. Nature Comms., DOI:10.1038/ncomms10113

Goodchild, S.C., Sheynis, T., Thompson, R., Tipping, K.W., Xue, W.F., Ranson, N.A., Beales, P.A., Hewitt, E.W. & Radford, S.E. (2014). β2-Microglobulin Amyloid Fibril-Induced Membrane Disruption Is Enhanced by Endosomal Lipids and Acidic pH. PLoS One, 9 (8), e104492


Skp is a multivalent chaperone of outer membrane proteins. Schiffrin, R., Calabrese, A.N., Devine, P.W.A., Harris, S.A., Ashcroft, A.E., Brockwell. D.J. & Radford, S.E. (2016) Nat. Struct. Mol. Biol. in press
FPOP-LC-MS/MS suggests differences in interaction sites of amphipols and detergents with outer membrane proteins. Watkinson, T.G., Calabrese, A.N., Ault, J,R., Radford, S.E. & Ashcroft, A.E. (2016) J. Am. Soc. Mass Spectrom., in press
Two-way communication between SecY and SecA suggests a Brownian ratchet mechanism for protein translocation. Allen, W.J., Corey, R.A., Oatley, P., Sessions, R.B., Baldwin, S.A., Radford, S.E., Tuma, R. & Collinson, I. (2016) Elife, 5, e15598
Substrate protein folds while it is bound to the ATP-independent chaperone Spy. Stull, F., Koldewey, P., Humes, J.R., Radford, S.E. & Bardwell, J.C.A. (2016) Nat. Struct. Mol. Biol. 1, 53-59

How good is research at University of Leeds in Biological Sciences?

FTE Category A staff submitted: 60.90

Research output data provided by the Research Excellence Framework (REF)

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