Crystallographic analysis of lmra, the bacterial homologue of the human multidrug resistence p-glycoprotein
FP5 — Improving Human Research Potential
- Duration
- 2002-02-01 → 2004-01-31
- EU contribution
- €114,272
- Participants
- 1
- Scheme
- RGI
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Project objective
LmrA from Lactococcus lactis is integral membrane ABC transporter, responsible for the extrusion of a variety of drugs from the inner leaflet of the cell. Our aim is to determine the crystal structure of LmrA in complex with non-hydrolyzable nucleotides and allosteric modulators. This structure would be the first for a complete ARC multidrug transporter. To perform a structural analysis through X -ray crystallography various subsequent steps must be satisfied: protein over expression and purification in quantities, protein crystallization, phase problem analysis and resolution, model building and refinement. I will take part to all these aspects of the experimental work and will be trained in the methodology and treatment of membrane proteins. This will be of great impact to me, given the scientific value of the project, but also the amount and quality of experimental work that I will have to perform. The impact to the host institution may be also quantified basing on the importance of the project from a scientific and bio-medical point of view. Membrane proteins have been and will continue to be the highest challenging objects of research in Structural Biology and the host laboratory will contribute to the advances in the field.
Original text from CORDIS.
Participants
- University of Cambridge · CambridgeCoordinatorUnited Kingdom
Links
Data: CORDIS, © European Union
