2003年
Association of alpha-subunits with nucleotide-modified beta-subunits induces asymmetry in the catalytic sites of the F-1-ATPase alpha(3)beta(3)-hexamer
CELL BIOCHEMISTRY AND BIOPHYSICS
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- 巻
- 39
- 号
- 3
- 開始ページ
- 175
- 終了ページ
- 181
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1385/CBB:39:3:175
- 出版者・発行元
- HUMANA PRESS INC
The photoaffinity spin-labeled ATP analog, 2-N-3-SL-adenosine triphosphate (ATP), was used to covalently modify isolated beta-subunits from F-1-ATPase of the thermophilic bacterium PS3. Approximately 1.2 mol of the nucleotide analog bound to the isolated subunit in the dark. Irradiation leads to covalent incorporation of the nucleotide into the binding site. ESR spectra of the complex show a signal that is typical for protein-immobilized radicals. Addition of isolated alpha-subunits to the modified beta-subunits results in ESR spectra with two new signals indicative of two distinctly different environments of the spin-label, e.g., two distinctly different conformations of the catalytic sites. The relative ratio of the signals is approx 2:1 in favor of the more closed conformation. The data show for the first time that when nucleotides are bound to isolated beta-subunits, binding of alpha-subunits induces asymmetry in the catalytic sites even in the absence of the gamma-subunit.
- リンク情報
- ID情報
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- DOI : 10.1385/CBB:39:3:175
- ISSN : 1085-9195
- PubMed ID : 14716074
- Web of Science ID : WOS:000187575200001