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Science 10 September 2004:
Vol. 305. no. 5690, pp. 1587 - 1594
DOI: 10.1126/science.1101952
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Research Articles

Mechanism of Ammonia Transport by Amt/MEP/Rh: Structure of AmtB at 1.35 Å

Shahram Khademi, Joseph O'Connell, III, Jonathan Remis, Yaneth Robles-Colmenares, Larry J. W. Miercke, Robert M. Stroud*

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 NH 4+/NH3, a binding site for NH 4+, and a 20 angstrom–long hydrophobic channel that lowers the NH 4+ pKa to below 6 and conducts NH3. Favorable interactions for NH3 are seen within the channel and use conserved histidines. Reconstitution of AmtB into vesicles shows that AmtB conducts uncharged NH3.

Department of Biochemistry and Biophysics, S412C Genentech Hall, University of California–San Francisco, 600 16th Street, San Francisco, CA 94143–2240, USA.

* To whom correspondence should be addressed. E-mail: stroud{at}msg.ucsf.edu

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