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Physiology 21: 419-429, 2006; doi:10.1152/physiol.00051.2005
1548-9213/06 $8.00
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Physiology, Vol. 21, No. 6, 419-429, December 2006
© 2006 Int. Union Physiol. Sci./Am. Physiol. Soc.

REVIEW

The Amt/MEP/Rh Family: Structure of AmtB and the Mechanism of Ammonia Gas Conduction

Shahram Khademi and Robert M. Stroud

Department of Biochemistry and Biophysics, University of California-San Francisco, San Francisco, California stroud{at}msg.ucsf.edu

The atomic structures of the first members of the Amt/MEP/Rh family show that they are 11-crossing membrane proteins that form trimers in the membrane. Each monomer supports a hydrophobic channel that conducts NH3 but not any water or ions. The reprotonation of NH3 on the receiving side raises the pH on that side in the absence of metabolism of NH3, and there is no transfer of protons through the protein.




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