Ontology highlight
ABSTRACT:
SUBMITTER: Hall JA
PROVIDER: S-EPMC3156211 | biostudies-literature | 2011 Aug
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20110720 32
In Escherichia coli, each subunit of the trimeric channel protein AmtB carries a hydrophobic pore for transport of NH(4)(+) across the cytoplasmic membrane. Positioned along this substrate conduction pathway are two conserved elements--a pair of hydrogen-bonded histidines (H168/H318) located within the pore itself and a set of aromatic residues (F107/W148/F215) at its periplasmic entrance--thought to be critical to AmtB function. Using site-directed mutagenesis and suppressor genetics, we examin ...[more]