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General conformational dynamics of heterodimeric ABC transporters

January 2017. ABC transporters shuttle chemically diverse substances across membranes in an energy-dependent manner. They mediate multidrug resistance in microorganisms and cancer cells and can cause human pathologies when dysfunctional. While important insights into ABC transporters have been gained in recent years, fundamental questions concerning their mechanism remain. Frankfurt scientists together with colleagues from the University of California, the Swiss Light source and Konstanz University has identified the protein complex TmrAB as a functional homolog of the antigenic peptide transporter TAP and present its high-resolution structure. This structure adopts an asymmetric conformational state and is characterized by C-terminal zipper helices that are essential for efficient substrate translocation. Together with functional studies the structure enabled the team to outline the general conformational dynamics of heterodimeric ABC transporters and to establish TmrAB as a model system for TAP. The study has been published on line in the Proceedings of the National Academy of Sciences of the USA on 9 January 2016. More ...

 

Contact:
Robert Tampé, Institute of Biochemistry, Campus Riedberg, Goethe University Frankfurt, Germany, Tel. +49 69 798-29475, tampe@em.uni-frankfurt.de

 

Publication:
Anne Nöll, Christoph Thomas, Valentina Herbring, Tina Zollmann, Katja Barth, Ahmad Reza Mehdipour, Thomas M. Tomasiak, Stefan Brüchert, Benesh Joseph, Rupert Abele, Vincent Oliéric, Meitian Wang, Kay Diederichs, Gerhard Hummer, Robert M. Stroud, Klaas M. Pos, and Robert Tampé. 2017. Crystal structure and mechanistic basis of a functional homolog of the antigen transporter TAP. PNAS, published ahead of print 9 January 2017, doi:10.1073/pnas.1620009114. Link