The c-ring stoichiometry of ATP synthase is adapted to cell physiological requirements of alkaliphilic Bacillus pseudofirmus OF4

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

Volumn 110, Issue 19, 2013, Pages 7874-7879

  Preiss, Laura ^a   Klyszejko, Adriana L ^a   Hicks, David B ^b   Liu, Jun ^b   Fackelmayer, Oliver J ^b   Yildiz, Özkan ^a   Krulwich, Terry A ^b   Meier, Thomas ^a,c  

^a MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^b MOUNT SINAI SCHOOL OF MEDICINE   (United States)

^c GOETHE UNIVERSITY   (Germany)

Author keywords

F1Fo ATP synthase rotor; Membrane protein complex

Indexed keywords

ALANINE; GLYCINE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

ARTICLE; ATOMIC FORCE MICROSCOPY; BACILLUS; BACILLUS PSEUDOFIRMUS; CELL FUNCTION; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; STOICHIOMETRY; X RAY CRYSTALLOGRAPHY;

F1FO-ATP SYNTHASE ROTOR; MEMBRANE PROTEIN COMPLEX;

ALANINE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACILLUS; CELL MEMBRANE; CRYSTALLOGRAPHY, X-RAY; GLYCINE; HYDROGEN-ION CONCENTRATION; MICROSCOPY, ATOMIC FORCE; MITOCHONDRIAL PROTON-TRANSLOCATING ATPASES; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 84877324079     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1303333110     Document Type: Article

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