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Structures of membrane transport proteins elucidated by crystallography and protein engineering


Research objectives and content
The mechanism of solute translocation across biological membranes is a fundamental and unresolved problem of modern biology. I intend to contribute to this field by investigating the structure/functic relationship of the arabinose-H+ symporter from Escherichia cold and the mj1560 multidrug efflux protein from Methanococcus jannaschii. Both proteins are already successfully over expressed in E. cold and canbe purified in satisfactorily amounts necessary for structure determination. Structure elucidation will be performed mainly by crystallization of the proteins in three dimensions followed by X-ray diffraction, but perhaps also in two dimensions followed by electron diffraction. If time permits, structure/function relationships of the arabinose-H+ symporter will be studied using fusions between this protein and the homologous galactose-H+ symporter GalP from E. coli.
Training content (objective, benefit and expected impact)
With the training in three-dimensional crystallization techniques and the use of other alternative strategic,(e.g. two-dimensional
crystallization), the proposed stay in the laboratory of Prof. Henderson will be a natural and very attractive complementation of my existing experimental skills. It will be necessary to have these skills in order to tackle in future the major unresolved problem in the field of membrane biology i.e. the mechanism of solute translocation across biological membranes.
Links with industry / industrial relevance (22) The host institution has support from Smithkline-Beecham,Glaxo-Wellcome and Sanofi for the delevelopment of antimicrobials in related research projects.

Funding Scheme

RGI - Research grants (individual fellowships)


Woodhouse Lane
LS2 9JT Leeds - West Yorkshire
United Kingdom