Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation

  title={Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation},
  author={Michael Hohl and Christophe Briand and Markus G. Gruetter and Markus A Seeger},
  journal={Nature Structural &Molecular Biology},
ATP-binding cassette (ABC) transporters shuttle a wide variety of molecules across cell membranes by alternating between inward- and outward-facing conformations, harnessing the energy of ATP binding and hydrolysis at their nucleotide binding domains (NBDs). Here we present the 2.9-Å crystal structure of the heterodimeric ABC transporter TM287–TM288 (TM287/288) from Thermotoga maritima in its inward-facing state. In contrast to previous studies, we found that the NBDs only partially separate… CONTINUE READING
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