The pivotal twin histidines and aromatic triad of the Escherichia coli ammonium channel AmtB can be replaced

Proceedings of the National Academy of Sciences of the United States of America

Volumn 108, Issue 32, 2011, Pages 13270-13274

  Hall, Jason A ^a   Kustu, Sydney ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Ammonium transport; Amt proteins; Enteric bacteria; Membrane channels

Indexed keywords

ALIPHATIC COMPOUND; AMMONIA; AROMATIC AMINO ACID; BACTERIAL PROTEIN; HISTIDINE; ION CHANNEL; PROTEIN AMTB; UNCLASSIFIED DRUG;

ARTICLE; CELL MEMBRANE; CONTROLLED STUDY; ESCHERICHIA COLI; HYDROGEN BOND; ION TRANSPORT; MEMBRANE CHANNEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; SITE DIRECTED MUTAGENESIS; SUPPRESSOR GENE; WILD TYPE;

AMINO ACIDS; CATION TRANSPORT PROTEINS; ESCHERICHIA COLI K12; ESCHERICHIA COLI PROTEINS; HISTIDINE; MUTANT PROTEINS; PROTEIN TRANSPORT; QUATERNARY AMMONIUM COMPOUNDS;

ENTEROBACTERIACEAE; ESCHERICHIA COLI;

EID: 80052019711     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1108451108     Document Type: Article

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