Nature Communications (May 2016)

A conserved leucine occupies the empty substrate site of LeuT in the Na+-free return state

  • Lina Malinauskaite,
  • Saida Said,
  • Caglanur Sahin,
  • Julie Grouleff,
  • Azadeh Shahsavar,
  • Henriette Bjerregaard,
  • Pernille Noer,
  • Kasper Severinsen,
  • Thomas Boesen,
  • Birgit Schiøtt,
  • Steffen Sinning,
  • Poul Nissen

DOI
https://doi.org/10.1038/ncomms11673
Journal volume & issue
Vol. 7, no. 1
pp. 1 – 11

Abstract

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Neurotransmitter:sodium symporters (NSS) perform Na+-dependent amino-acid uptake, but a full structural description of their function is lacking. Here the authors present a structure of the bacterial NSS LeuT in the outward-oriented empty state and show that a Leu residue occupies the empty substrate site and is essential for function.