MEMBRANE PROTEIN CRYSTALLOGRAPHY
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 in the structural and functional characterisation of multidrug membrane transporters by X-ray crystallography.
The lab is based at the Research Complex at Harwell, Oxfordshire (https://www.rc-harwell.ac.uk/research-groups/beis-group/).
We are 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 interested to understand how ABC transporters recognise their substrates as well as the conformational changes associated with ATP and substrate binding, as well as ATP hydrolysis. We employ protein crystallography, transport assays and biophysical methods such as PELDOR/EPR and smFRET.
et al., Desolvation of the substrate binding protein TauA dictates ligand specificity for the alkanesulfonate ABC importer TauABC, Biochemical Journal, ISSN:0264-6021
Beis K, Rebuffat S, 2019, Multifaceted ABC transporters associated to microcin and bacteriocin export, Research in Microbiology, Vol:170, ISSN:0923-2508, Pages:399-406
et al., 2019, OmpK36-mediated Carbapenem resistance attenuates ST258 Klebsiella pneumoniae in vivo, Nature Communications, Vol:10, ISSN:2041-1723
et al., 2019, Crystal structure and epitope analysis of house dust mite allergen Der f 21, Scientific Reports, Vol:9, ISSN:2045-2322
et al., 2019, Solid immersion microscopy images cells under cryogenic conditions with 12 nm resolution, Communications Biology, Vol:2, ISSN:2399-3642