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      Mechanistic diversity in ATP-binding cassette (ABC) transporters.

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      Nature structural & molecular biology

      Springer Nature

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          Abstract

          ABC transporters catalyze transport reactions, such as the high-affinity uptake of micronutrients into bacteria and the export of cytotoxic compounds from mammalian cells. Crystal structures of ABC domains and full transporters have provided a framework for formulating reaction mechanisms of ATP-driven substrate transport, but recent studies have suggested remarkable mechanistic diversity within this protein family. This review evaluates the differing mechanistic proposals and outlines future directions for the exploration of ABC-transporter-catalyzed reactions.

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          Author and article information

          Journal
          Nat. Struct. Mol. Biol.
          Nature structural & molecular biology
          Springer Nature
          1545-9985
          1545-9985
          Jun 07 2016
          : 23
          : 6
          Affiliations
          [1 ] Institute of Molecular Biology and Biophysics, Department of Biology, ETH Zurich, Zurich, Switzerland.
          Article
          nsmb.3216
          10.1038/nsmb.3216
          27273632
          1da6df4e-ff71-42d4-9ae5-26d19ad045a3

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