Identification of α‐subunit Lys201 and β‐subunit Lys115 at the ATP‐binding sites inEscherichia coli F1‐ATPase

FEBS Letters

Futai, Masamitsu¹  Tagaya, Mitsuo¹  Noumi, Takato¹  Nakano, Kenichi¹  Fukui, Toshio¹ 

[1] Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567, Japan

关键词: F1-ATPase;    Nucleotide-binding site;    Affinity label;    Adenosine polyphosphopyridoxal;    Glycine-rich region;    AP3-PL;    adenosine triphosphopyridoxal;    FSBA;    5′-p-fluorosulfonylbenzoyl adenosine;    FSBI;    5′-p-fluorosulfonylbenzoyl inosine;    HPLC;    high performance liquid chromatography;   

DOI  :  10.1016/0014-5793(88)80457-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Binding of about 1 mol of adenosine triphosphopyridoxal to Escherichia coli F₁-ATPase resulted in the nearly complete inactivation of the enzyme [(1987) J. Biol. Chem. 262, 7686–7692]. About two thirds of the label was bound to the α-subunit, and the rest to the β-subunit. The present study revealed that Lys²⁰¹ in the α-subunit and Lys¹⁵⁵ in the glycinerich region of the β-subunit are the major sites labeled with this reagent. Thus, these two residues might be located close to the γ-phosphate of the bound ATP.

【 授权许可】

Unknown