Catalytic and noncatalytic nucleotide binding sites of the Escherichia coli F1 ATPase Amino acid sequences of β‐subunit tryptic peptides labeled with 2‐azido‐ATP

FEBS Letters

Wise, John G.¹  Boyer, Paul D.¹  Hicke, Brian J.¹ 

[1] Department of Chemistry and Biochemistry and Molecular Biology Institute, University of California, Los Angeles, CA 90024-1570, USA

关键词: H+-ATPase;    Oxidative phosphorylation;    Photoaffinity analog;    Azido-ATP;    (E. coli);   

DOI  :  10.1016/0014-5793(87)80326-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Under appropriate conditions tight, noncovalent binding of 2-azido-adenine nucleotides to either catalytic or noncatalytic binding sites on the E. coli F₁-ATPase occurs. After removal of unbound ligands, UV-irradiation results primarily in the covalent incorporation of nucleotide moieties into the β-subunit in both catalytic and noncatalytic site labeling experiments. Minor labeling of the α-subunit was also observed. After trypsin digestion and purification of the labeled peptides, microsequencing studies identified two adjacent β-subunit tryptic peptides labeled by 2-azido-ADP or -ATP. These β-subunit peptides were labeled on tyrosine-331 (catalytic sites) and tyrosine-354 (noncatalytic sites) in homology with the labeling patterns of the mitochondrial and chloroplast enzymes.

【 授权许可】

Unknown