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Mechanism of Ammonia Transport by Amt/MEP/Rh: Structure of AmtB at 1.35 Å
Abstract
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 + /NH 3 , a binding site for NH 4 + , and a 20 angstrom–long hydrophobic channel that lowers the NH 4 + p K a to below 6 and conducts NH 3 . Favorable interactions for NH 3 are seen within the channel and use conserved histidines. Reconstitution of AmtB into vesicles shows that AmtB conducts uncharged NH 3 .
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Metadata
- Authors
- Khademi, S., O'Connell, J., Remis, J., Robles-Colmenares, Y., Miercke, L. J. W., & Stroud, R. M.
- Venue
- Science
- Published
- 2004-09-10
- Volume
- 305
- Issue
- 5690
- Pages
- 1587-1594
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1995087505
- Cited by
- 667
- References
- 0
- FWCI
- 27.82
- Type
- journal article
- Language
- en
- Open access
- closed
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- Khademi, S., O'Connell, J., Remis, J., Robles-Colmenares, Y., Miercke, L. J. W., & Stroud, R. M. (2004). Mechanism of Ammonia Transport by Amt/MEP/Rh: Structure of AmtB at 1.35 Å. Science. https://doi.org/10.1126/science.1101952
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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