期刊
SCIENCE
卷 305, 期 5690, 页码 1587-1594出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1101952
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资金
- NIGMS NIH HHS [GM24485] Funding Source: Medline
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 NH4+/NH3, a binding site for NH4+, and a 20 angstrom-long hydrophobic channel that lowers the NH4+ pK(a) 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.
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