| Literature DB >> 16842212 |
Massoud Saidijam1, Giulia Benedetti, Qinghu Ren, Zhiqiang Xu, Christopher J Hoyle, Sarah L Palmer, Alison Ward, Kim E Bettaney, Gerda Szakonyi, Johan Meuller, Scott Morrison, Martin K Pos, Patrick Butaye, Karl Walravens, Kate Langton, Richard B Herbert, Ronald A Skurray, Ian T Paulsen, John O'reilly, Nicholas G Rutherford, Melissa H Brown, Roslyn M Bill, Peter J F Henderson.
Abstract
Drug efflux proteins are widespread amongst microorganisms, including pathogens. They can contribute to both natural insensitivity to antibiotics and to emerging antibiotic resistance and so are potential targets for the development of new antibacterial drugs. The design of such drugs would be greatly facilitated by knowledge of the structures of these transport proteins, which are poorly understood, because of the difficulties of obtaining crystals of quality. We describe a structural genomics approach for the amplified expression, purification and characterisation of prokaryotic drug efflux proteins of the 'Major Facilitator Superfamily' (MFS) of transport proteins from Helicobacter pylori, Staphylococcus aureus, Escherichia coli, Enterococcus faecalis, Bacillus subtilis, Brucella melitensis, Campylobacter jejuni, Neisseria meningitides and Streptomyces coelicolor. The H. pylori putative drug resistance protein, HP1092, and the S. aureus QacA proteins are used as detailed examples. This strategy is an important step towards reproducible production of transport proteins for the screening of drug binding and for optimisation of crystallisation conditions to enable subsequent structure determination.Entities:
Mesh:
Substances:
Year: 2006 PMID: 16842212 DOI: 10.2174/138945006777709575
Source DB: PubMed Journal: Curr Drug Targets ISSN: 1389-4501 Impact factor: 3.465