The A-type ATP synthase subunit K of Methanopyrus kandleri is deduced from its sequence to form a monomeric rotor comprising 13 hairpin domains

FEBS Letters

Volumn 543, Issue 1-3, 2003, Pages 47-50

  Lolkema, Juke S ^a   Boekema, Egbert J ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

A ATP synthase; Hyperthermophile; Methanopyrus kandleri; Ring structure; Rotor; Subunit c

Indexed keywords

CATION; GENE PRODUCT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARCHAEBACTERIUM; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME SUBUNIT; METHANOPYRUS KANDLERI; NONHUMAN; PAIRED HELICAL FILAMENT; PRIORITY JOURNAL; PROTEIN DOMAIN;

ARCHAEA; METHANOPYRUS KANDLERI;

EID: 0038731187     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(03)00398-3     Document Type: Article

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