Roles of the β subunit hinge domain in ATP synthase F1 sector: Hydrophobic network formed by introduced βPhe174 inhibits subunit rotation

Biochemical and Biophysical Research Communications

Volumn 395, Issue 2, 2010, Pages 173-177

  Nakanishi Matsui, Mayumi ^a   Kashiwagi, Sachiko ^a   Kojima, Masaki ^b   Nonaka, Takamasa ^a   Futai, Masamitsu ^a  

^a IWATE MEDICAL UNIVERSITY   (Japan)

^b TOKYO UNIVERSITY OF PHARMACY AND LIFE SCIENCES   (Japan)

Author keywords

Subunit; ATP synthase; F1; Modeling; Rotation; Ser174

Indexed keywords

ALANINE; GLYCINE; ISOLEUCINE; METHIONINE; PHENYLALANINE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE BETA; SERINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; COMPUTER PROGRAM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBUNIT; ESCHERICHIA COLI; EXPERIMENTAL MODEL; GENE MUTATION; HYDROPHOBICITY; PREDICTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; SEQUENCE HOMOLOGY;

AMINO ACID SUBSTITUTION; ATP SYNTHETASE COMPLEXES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROPHOBICITY; MEMBRANE PROTEINS; MUTATION; PHENYLALANINE; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; ROTATION; TRANSCRIPTION FACTORS;

ESCHERICHIA COLI;

EID: 77951622938     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.03.127     Document Type: Article

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