Arg-302 facilitates deprotonation of Glu-325 in the transport mechanism of the lactose permease from Escherichia coli

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

Volumn 98, Issue 11, 2001, Pages 6068-6073

  Sahin Tóth, Miklós ^a   Kaback, H Ronald ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CARBOXYLIC ACID; GLUTAMIC ACID; HISTIDINE; LACTOSE; LACTOSE PERMEASE; LIGAND; PROTON;

ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; EQUILIBRIUM CONSTANT; ESCHERICHIA COLI; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTON TRANSPORT;

ARGININE; BIOLOGICAL TRANSPORT; BIOLOGICAL TRANSPORT, ACTIVE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GLUTAMIC ACID; LACTOSE; MEMBRANE TRANSPORT PROTEINS; MONOSACCHARIDE TRANSPORT PROTEINS; MUTAGENESIS; NITROPHENYLGALACTOSIDES; PROTONS; SUBSTRATE SPECIFICITY; SYMPORTERS;

BACTERIA (MICROORGANISMS); EARIAS; ESCHERICHIA COLI;

EID: 0035932954     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.111139698     Document Type: Article

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