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Understanding ATP synthase regulation


EMSL Project ID
50619

Abstract

We aim to solve the cryo-EM structure of E. coli ATP synthase in its active form to high resolution utilising the PNCC Titan Krios equipped with a K2 camera. This research will be an extension of our previous work describing the same enzyme in an inhibited form (Sobti et al 2016). The knowledge gained here will further our fundamental understanding of the function and regulation of this essential biological molecule, as well as potentially leading to future antimicrobial development.

Project Details

Start Date
2018-12-01
End Date
2019-07-31
Status
Closed

Team

Principal Investigator

Alastair Stewart
Institution
The Victor Chang Cardiac Research Institute

Team Members

Meghna Sobti
Institution
The Victor Chang Cardiac Research Institute

Claudia Lopez
Institution
Oregon Health & Science University

Related Publications

Sobti M., J.L. Walshe, D. Wu, R. Ishmukhametov, Y.C. Zeng, C.V. Robinson, and R.M. Berry, et al. 2020. "Cryo-EM Structures Provide Insight Into How E. coli F1Fo ATP Synthase Accommodates Symmetry Mismatch." Nature Communications 11.
Sobti M., J.L. Walshe, R. Ishmukhametov, and A.G. Stewart. 2019. "Visualizing Movements in E. Coli F1Fo ATP Synthase Indicates How the F1and Fo Motors are Coupled." bioRxiv. doi:10.1101/622084