Ammonia transporter
| Ammonia transporter | |||||||||
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| Identifiers | |||||||||
| Symbol | AmtB | ||||||||
| Pfam | PF00909 | ||||||||
| InterPro | IPR001905 | ||||||||
| TCDB | 1.A.11 | ||||||||
| OPM superfamily | 13 | ||||||||
| OPM protein | 2ns1 | ||||||||
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| Available protein structures: | |
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| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
Ammonia transporters (TC# 1.A.11) are structurally related membrane transport proteins called Amt proteins (ammonia transporters) in bacteria and plants, methylammonium/ammonium permeases (MEPs) in yeast, or Rhesus (Rh) proteins in chordates. In humans, the RhAG, RhBG, and RhCG Rhesus proteins constitute solute carrier family 42 whilst RhD and RhCE form the Rh blood group system. The three-dimensional structure of the ammonia transport protein AmtB from Escherichia coli has been determined by x-ray crystallography revealing a hydrophobic ammonia channel. The human RhCG ammonia transporter was found to have a similar ammonia-conducting channel structure. It was proposed that the erythrocyte Rh complex is a heterotrimer of RhAG, RhD, and RhCE subunits in which RhD and RhCE might play roles in anchoring the ammonia-conducting RhAG subunit to the cytoskeleton. Based on reconstitution experiments, purified RhCG subunits alone can function to transport ammonia. RhCG is required for normal acid excretion by the mouse kidney and epididymis.
The structure of the ammonia channel from E. coli, was, at the time of its publication, the highest resolution structure of any integral membrane protein. It shows a trimer of subunits, each made up of 11 transmembrane segments (TMSs) and containing a pseudo two-fold symmetry. Each monomer contains a hydrophobic ammonia conducting channel.
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