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-Structure paper
タイトル | Structural basis of unisite catalysis of bacterial FF-ATPase. |
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ジャーナル・号・ページ | PNAS Nexus, Vol. 1, Issue 3, Page pgac116, Year 2022 |
掲載日 | 2022年7月11日 |
著者 | Atsuki Nakano / Jun-Ichi Kishikawa / Atsuko Nakanishi / Kaoru Mitsuoka / Ken Yokoyama / |
PubMed 要旨 | Adenosine triphosphate (ATP) synthases (FF-ATPases) are crucial for all aerobic organisms. F, a water-soluble domain, can catalyze both the synthesis and hydrolysis of ATP with the rotation of the ...Adenosine triphosphate (ATP) synthases (FF-ATPases) are crucial for all aerobic organisms. F, a water-soluble domain, can catalyze both the synthesis and hydrolysis of ATP with the rotation of the central rotor inside a cylinder made of in three different conformations (referred to as , , and ). In this study, we determined multiple cryo-electron microscopy structures of bacterial FF exposed to different reaction conditions. The structures of nucleotide-depleted FF indicate that the ε subunit directly forces to adopt a closed form independent of the nucleotide binding to . The structure of FF under conditions that permit only a single catalytic subunit per enzyme to bind ATP is referred to as unisite catalysis and reveals that ATP hydrolysis unexpectedly occurs on instead of , where ATP hydrolysis proceeds in the steady-state catalysis of FF. This indicates that the unisite catalysis of bacterial FF significantly differs from the kinetics of steady-state turnover with continuous rotation of the shaft. |
リンク | PNAS Nexus / PubMed:36741449 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.6 - 4.5 Å |
構造データ | EMDB-33251, PDB-7xkh: EMDB-33252: Nucleotide-depleted F1 domain of FoF1-ATPase from Bacillus PS3, , state2 EMDB-33253: Nucleotide-depleted FoF1-ATPase from Bacillus PS3, state3 EMDB-33258, PDB-7xko: EMDB-33259, PDB-7xkp: EMDB-33260: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1,unisite condition EMDB-33261: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2,nucleotide depleted EMDB-33262: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2,unisite condition EMDB-33263: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state3,unisite condition EMDB-33264, PDB-7xkq: EMDB-33265, PDB-7xkr: EMDB-33266: epsilon-inhibited FoF1-ATPase from Bacillus PS3 at saturated ATP-gamma-S condition, state1 EMDB-33267: epsilon-inhibited FoF1-ATPase from Bacillus PS3 at saturated ATP-gamma-S condition, state2 EMDB-33268: epsilon-inhibited FoF1-ATPase from Bacillus PS3 at saturated ATP-gamma-S condition, state3 EMDB-33269: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2',nucleotide depleted EMDB-33277: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1,nucleotide depleted EMDB-33278: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1,unisite condition EMDB-33279: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1',unisite condition EMDB-33280: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2,nucleotide depleted EMDB-33281: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2',nucleotide depleted EMDB-33282: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2,unisite condition EMDB-33283: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state3,unisite condition |
化合物 | ChemComp-PI: ChemComp-MG: ChemComp-ADP: ChemComp-ATP: |
由来 |
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キーワード | MOTOR PROTEIN / ATP synthase F1 ATPase FoF1 |