Amt/MEP/Rh proteins conduct ammonia

@article{Winkler2005AmtMEPRhPC,
  title={Amt/MEP/Rh proteins conduct ammonia},
  author={Fritz K. Winkler},
  journal={Pfl{\"u}gers Archiv},
  year={2005},
  volume={451},
  pages={701-707}
}
The structure determination of the ammonium transport protein AmtB from Escherichia coli strongly indicates that the members of the ubiquitous ammonium transporter/methylamine permease/Rhesus (Amt/MEP/Rh) protein family are ammonia-conducting channels rather than ammonium ion transporters. The most conserved part of these proteins, apart from the common overall structure with 11 transmembrane helices, is the pore lined by hydrophobic side chains except for two highly conserved histidine… CONTINUE READING
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Citations

Publications citing this paper.
SHOWING 1-10 OF 36 CITATIONS

Structural and mechanistic aspects of Amt/Rh proteins.

  • Journal of structural biology
  • 2007
VIEW 4 EXCERPTS
CITES BACKGROUND & RESULTS
HIGHLY INFLUENCED

Evolution of Electrogenic Ammonium Transporters (AMTs)

  • Front. Plant Sci.
  • 2016
VIEW 2 EXCERPTS
CITES METHODS & BACKGROUND

References

Publications referenced by this paper.
SHOWING 1-10 OF 49 REFERENCES

Characteristics of renal Rhbg as an NH4(+) transporter.

  • American journal of physiology. Renal physiology
  • 2005
VIEW 9 EXCERPTS
HIGHLY INFLUENTIAL

The crystal structure of AmtB of E. coli suggests a mechanism for ammonia transport

L Zheng, D Kostrewa, S Bernèche, FK Winkler, X-D Li
  • Proc Natl Acad Sci USA
  • 2004
VIEW 12 EXCERPTS
HIGHLY INFLUENTIAL

Aquaporin water channels (Nobel Lecture).

  • Angewandte Chemie
  • 2004
VIEW 1 EXCERPT

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