Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A.

@article{Khademi2004MechanismOA,
  title={Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A.},
  author={Shahram Khademi and Joseph O'Connell and Jonathan Remis and Yaneth Robles-Colmenares and Larry J. W. Miercke and Robert Michael Stroud},
  journal={Science},
  year={2004},
  volume={305 5690},
  pages={1587-94}
}
The first structure of an ammonia channel from the Amt/MEP/Rh protein superfamily, determined to 1.35 angstrom resolution, shows it to be a channel that spans the membrane 11 times. Two structurally similar halves span the membrane with opposite polarity. Structures with and without ammonia or methyl ammonia show a vestibule that recruits NH4+/NH3, a binding site for NH4+, and a 20 angstrom-long hydrophobic channel that lowers the NH4+ pKa to below 6 and conducts NH3. Favorable interactions for… CONTINUE READING
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