MEMBRANE PROTEIN STRUCTURAL BIOLOGY
The lab is based at the Research Complex at Harwell, Oxfordshire (https://www.rc-harwell.ac.uk/research-groups/beis-group/).
Membrane proteins represent around 30% of the proteomes of most organisms and more than 40% of drug targets and yet few structures of these molecules have been solved by x-ray crystallography. Drug resistance of bacterial pathogens is a rising crisis. Bacterial membrane proteins are essential for resistance since they are involved in the export of the drugs from the cell. My group is interested to determine the structure and function of these proteins in order to elucidate the molecular mechanism of drug resistance.
The lab is also interested to exploit novel antibacterials as treatments for bacterial infections by understanding how bacteria secrete antibacterial peptides and hijack membrane transporters of other bacteria to inhibit their growth under nutrient starvation.
We are also investigating the mechanism and dynamics of ABC transporters by employing a multidisplinary approach of protein crystallography, transport assays and biophysical methods such as PELDOR/EPR and smFRET.
et al., 2022, Mating pair stabilization mediates bacterial conjugation species specificity, Nature Microbiology, ISSN:2058-5276
et al., 2021, Molecular mechanism of SbmA, a promiscuous transporter exploited by antimicrobial peptides, Science Advances, Vol:7, ISSN:2375-2548, Pages:1-10
et al., 2020, Experimental phasing with vanadium and application to nucleotide-binding membrane proteins, Iucrj, Vol:7, ISSN:2052-2525, Pages:1092-1101
et al., 2022, Stabilizing bacterial conjugation via conjugation junction proteins, CELL PRESS, Pages:462A-462A, ISSN:0006-3495