Structural studies of a bacterial membrane bound antibiotic transporter

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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. Bacterial membrane proteins are essential for antibiotic resistance since they are involved in the export of the drugs from the cell. These proteins are usually embedded in oil like environment making them very difficult to work with. We first need to isolate them from the membrane using lipid mimics such as detergents. Membrane proteins usually have many functions and bacteria have developed mechanisms to utilise them in order to extrude antibiotics through these proteins. Understanding the structure and function of these important biological molecules will contribute to the understanding of the relationship between membrane protein and substrate recognition and provide valuable information to structural biology and pharmacology. In order to gain a detailed understanding of the mechanism of these proteins we need to grow crystals and expose them to X-rays in order to obtain the molecular structure. We have obtained such crystals of a bacterial membrane protein antibiotic transporter. The structural information of this membrane protein will provide an important insight on the binding and recognition of antibiotics from this new family of proteins. We are also going to understand the biochemistry of this protein in the presence of antibiotics. Having all these information, the structure and biochemical analysis, will have pharmacological importance since it will allow the development of novel antibiotics that can fight bacterial resistance.