The conserved dipole in transmembrane helix 5 of KdpB in the Escherichia coli KdpFABC P-type ATPase is crucial for coupling and the electrogenic K +-translocation step

Biochemistry

Volumn 46, Issue 48, 2007, Pages 13920-13928

  Becker, Doris ^a   Féndler, Klaus ^b   Altendorf, Karlheinz ^a   Greie, Jörg Christian ^a  

^a UNIVERSITY OF OSNABRÜCK   (Germany)

^b MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CHARGED RESIDUES; ELECTROGENIC REACTION; ENERGY COUPLINGS; K586 MUTANTS; POSITIVE CHARGE;

ADENOSINETRIPHOSPHATE; CATALYST ACTIVITY; CELL MEMBRANES; LIPID BILAYERS; LIPOSOMES; MUTAGENESIS;

ESCHERICHIA COLI;

ADENOSINE TRIPHOSPHATASE; KDPFABC PROTEIN; ORTHOVANADIC ACID; POTASSIUM; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CELL GROWTH; CELL TYPE; CONTROLLED STUDY; DIPOLE; ELECTRICITY; ELECTROPHYSIOLOGY; ENERGY METABOLISM; ENZYME ACTIVITY; ENZYME MECHANISM; GROWTH RATE; HYDROLYSIS; LIPID BILAYER; MOLECULAR DYNAMICS; MUTAGENESIS; NONHUMAN; POTASSIUM TRANSPORT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN QUATERNARY STRUCTURE; PROTEOLIPOSOME; SIGNAL TRANSDUCTION; TRANSMEMBRANE HELIX 5; WILD TYPE;

ADENOSINE TRIPHOSPHATASES; CATION TRANSPORT PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENETIC COMPLEMENTATION TEST; ION TRANSPORT; PLASMIDS; POTASSIUM; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI;

EID: 36849045167     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701394h     Document Type: Article

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