The role of the βDELSEED-loop of ATP synthase

Journal of Biological Chemistry

Volumn 284, Issue 17, 2009, Pages 11336-11345

  Mnatsakanyan, Nelli ^a   Krishnakumar, Arathianand M ^a   Suzuki, Toshiharu ^b   Weber, Joachim ^a  

^a TEXAS TECH UNIVERSITY   (United States)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ARRHENIUS ANALYSIS; ATP HYDROLYSIS; ATP SYNTHASE; ATP SYNTHESIS; C-TERMINAL DOMAINS; CATALYTIC SITES; CHEMICAL ENERGY; DELETION MUTANTS; HELIX-TURN-HELIX MOTIFS; HIGH-AFFINITY SITES; MECHANICAL ENERGIES; MECHANOCHEMICAL COUPLINGS; MEMBRANE PREPARATION; MEMBRANE VESICLES; NUCLEOTIDE BINDING; RATE LIMITING; TRANSMEMBRANE PROTON GRADIENT; WILD-TYPE ENZYMES;

AMINES; AMINO ACIDS; BACTERIOLOGY; BINDING SITES; HYDROLYSIS; MECHANISMS; ORGANIC ACIDS;

ENZYMES;

ADENOSINE TRIPHOSPHATE MAGNESIUM; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; ADENOSINE TRIPHOSPHATE; F1F0 ATP SYNTHASE; F1F0-ATP SYNTHASE; NUCLEOTIDE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

AMINO ACID COMPOSITION; ARTICLE; BACILLUS; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; DELETION MUTANT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; PROTEIN MOTIF; STRUCTURE ACTIVITY RELATION; THERMOPHILIC BACTERIUM; WILD TYPE; AMINO ACID SEQUENCE; BINDING SITE; CELL MEMBRANE; CHEMISTRY; CONFORMATION; METABOLISM; MOLECULAR GENETICS; MUTATION; PHOSPHORYLATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ATP SYNTHETASE COMPLEXES; BACILLUS; BINDING SITES; CELL MEMBRANE; ESCHERICHIA COLI; MITOCHONDRIAL PROTON-TRANSLOCATING ATPASES; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEOTIDES; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 66449113027     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M900374200     Document Type: Article

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