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Journal of Biological Chemistry

Volumn 281, Issue 51, 2006, Pages 39492-39498

An unusual twin-his arrangement in the pore of ammonia channels is essential for substrate conductance

(6) Javelle, Arnaud a,b Lupo, Domenico b Zheng, Lei b Li, Xiao Dan b Winkler, Fritz K b Merrick, Mike a

a JOHN INNES CENTRE (United Kingdom)

b PAUL SCHERRER INSTITUTE (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA CHANNELS; HOMOTRIMERS;

AMMONIA; CRYSTAL STRUCTURE; ESCHERICHIA COLI; FUNGI; SUBSTITUTION REACTIONS; SUBSTRATES;

PROTEINS;

GLUTAMATE AMMONIA LIGASE; GLUTAMIC ACID; HISTIDINE; MEMBRANE PROTEIN; PROTEIN AMTB; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN INTERACTION; WESTERN BLOTTING;

AMINO ACID SEQUENCE; AMMONIA; CATION TRANSPORT PROTEINS; ELECTRONS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENOTYPE; HISTIDINE; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEOTIDYLTRANSFERASES; PII NITROGEN REGULATORY PROTEINS; PLASMIDS; PROTEIN BINDING; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI; FUNGI;

EID: 33845981511 PISSN: 00219258 EISSN: 1083351X Source Type: Journal
DOI: 10.1074/jbc.M608325200 Document Type: Article

Times cited : (66)

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