ATP Binding to the KTN/RCK subunit KtrA from the K+-uptake system KtrAB of Vibrio alginolyticus: Its role in the formation of the KtrAB complex and its requirement in vivo

Journal of Biological Chemistry

Volumn 282, Issue 19, 2007, Pages 14018-14027

  Kröning, Nadine ^a   Willenborg, Marion ^a,b   Tholema, Nancy ^a,c   Hänelt, Inga ^a   Schmid, Roland ^a   Bakker, Evert P ^a  

^a UNIVERSITY OF OSNABRÜCK   (Germany)

^b UNIVERSITY OF KIEL   (Germany)

^c UNIVERSITY OF MÜNSTER   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALGINOLYTICUS; CYTOPLASMIC SIDE; UPTAKE SYSTEM;

AMINO ACIDS; BINDING SITES; CELL MEMBRANES; CHROMATOGRAPHIC ANALYSIS; CONCENTRATION (PROCESS); NUCLEOTIDES; PROTEINS;

BACTERIA;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AGAROSE; AMINO ACID; KTN PROTEIN; KTRA PROTEIN; KTRAB PROTEIN; NICKEL; NICOTINAMIDE ADENINE DINUCLEOTIDE; NUCLEOTIDE; POLYHISTIDINE TAG; POTASSIUM; PROTEIN DERIVATIVE; PROTEIN SUBUNIT; RCK PROTEIN; TRYPSIN; UNCLASSIFIED DRUG; BACTERIAL POLYSACCHARIDE; BACTERIAL PROTEIN; CATION TRANSPORT PROTEIN; HISTIDINE; KTRA POTASSIUM TRANSPORT PROTEIN, BACTERIA; KTRB PROTEIN, BACTERIA; MEMBRANE PROTEIN; PNEUMOCOCCAL POLYSACCHARIDE TYPE 1;

AFFINITY CHROMATOGRAPHY; ARTICLE; BACTERIAL CELL; CONFORMATION; CROSS LINKING; CYTOPLASM; DIALYSIS; ESCHERICHIA COLI; EXPERIMENT; GENE DELETION; IN VIVO STUDY; MEMBRANE POTENTIAL; NONHUMAN; POTASSIUM TRANSPORT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN ISOLATION; VIBRIO ALGINOLYTICUS; CELL MEMBRANE; CELL MEMBRANE POTENTIAL; CHEMISTRY; COMPARATIVE STUDY; GENETICS; METABOLISM;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; VIBRIO ALGINOLYTICUS;

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; CATION TRANSPORT PROTEINS; CELL MEMBRANE; CHROMATOGRAPHY, AFFINITY; CYTOPLASM; ESCHERICHIA COLI; HISTIDINE; MEMBRANE POTENTIALS; MEMBRANE PROTEINS; POLYSACCHARIDES, BACTERIAL; POTASSIUM; PROTEIN SUBUNITS; SEQUENCE DELETION; VIBRIO ALGINOLYTICUS;

EID: 34347257454     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M609084200     Document Type: Article

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