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1MAB

RAT LIVER F1-ATPASE

1MAB の概要
エントリーDOI10.2210/pdb1mab/pdb
分子名称PROTEIN (F1-ATPASE ALPHA CHAIN), PROTEIN (F1-ATPASE BETA CHAIN), PROTEIN (F1-ATPASE GAMMA CHAIN), ... (8 entities in total)
機能のキーワードatp synthase, fof1-atpase, oxidative phosphorylation, mitochondria, hydrolase
由来する生物種Rattus norvegicus (Norway rat)
詳細
細胞内の位置Mitochondrion inner membrane : P15999
Mitochondrion: P10719 P35435
タンパク質・核酸の鎖数3
化学式量合計137780.73
構造登録者
Bianchet, M.A.,Amzel, L.M. (登録日: 1998-08-06, 公開日: 1998-09-30, 最終更新日: 2024-05-22)
主引用文献Bianchet, M.A.,Hullihen, J.,Pedersen, P.L.,Amzel, L.M.
The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis.
Proc.Natl.Acad.Sci.USA, 95:11065-11070, 1998
Cited by
PubMed Abstract: During mitochondrial ATP synthesis, F1-ATPase-the portion of the ATP synthase that contains the catalytic and regulatory nucleotide binding sites-undergoes a series of concerted conformational changes that couple proton translocation to the synthesis of the high levels of ATP required for cellular function. In the structure of the rat liver F1-ATPase, determined to 2.8-A resolution in the presence of physiological concentrations of nucleotides, all three beta subunits contain bound nucleotide and adopt similar conformations. This structure provides the missing configuration of F1 necessary to define all intermediates in the reaction pathway. Incorporation of this structure suggests a mechanism of ATP synthesis/hydrolysis in which configurations of the enzyme with three bound nucleotides play an essential role.
PubMed: 9736690
DOI: 10.1073/pnas.95.19.11065
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.8 Å)
構造検証レポート
Validation report summary of 1mab
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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