Structural analysis of ATP bound to the F1-ATPase β-subunit monomer by solid-state NMR- insight into the hydrolysis mechanism in F1
Copyright © 2024 Elsevier B.V. All rights reserved..
ATP-hydrolysis-associated conformational change of the β-subunit during the rotation of F1-ATPase (F1) has been discussed using cryo-electron microscopy (cryo-EM). Since it is worthwhile to further investigate the conformation of ATP at the catalytic subunit through an alternative approach, the structure of ATP bound to the F1β-subunit monomer (β) was analyzed by solid-state NMR. The adenosine conformation of ATP-β was similar to that of ATP analog in F1 crystal structures. 31P chemical shift analysis showed that the Pα and Pβ conformations of ATP-β are gauche-trans and trans-trans, respectively. The triphosphate chain is more extended in ATP-β than in ATP analog in F1 crystals. This appears to be in the state just before ATP hydrolysis. Furthermore, the ATP-β conformation is known to be more closed than the closed form in F1 crystal structures. In view of the cryo-EM results, ATP-β would be a model of the most closed β-subunit with ATP ready for hydrolysis in the hydrolysis stroke of the F1 rotation.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:309 |
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| Enthalten in: |
Biophysical chemistry - 309(2024) vom: 09. Apr., Seite 107232 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Todokoro, Yasuto [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 22.04.2024 Date Revised 22.04.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.bpc.2024.107232 |
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| 245 | 1 | 0 | |a Structural analysis of ATP bound to the F1-ATPase β-subunit monomer by solid-state NMR- insight into the hydrolysis mechanism in F1 |
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| 500 | |a Date Revised 22.04.2024 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2024 Elsevier B.V. All rights reserved. | ||
| 520 | |a ATP-hydrolysis-associated conformational change of the β-subunit during the rotation of F1-ATPase (F1) has been discussed using cryo-electron microscopy (cryo-EM). Since it is worthwhile to further investigate the conformation of ATP at the catalytic subunit through an alternative approach, the structure of ATP bound to the F1β-subunit monomer (β) was analyzed by solid-state NMR. The adenosine conformation of ATP-β was similar to that of ATP analog in F1 crystal structures. 31P chemical shift analysis showed that the Pα and Pβ conformations of ATP-β are gauche-trans and trans-trans, respectively. The triphosphate chain is more extended in ATP-β than in ATP analog in F1 crystals. This appears to be in the state just before ATP hydrolysis. Furthermore, the ATP-β conformation is known to be more closed than the closed form in F1 crystal structures. In view of the cryo-EM results, ATP-β would be a model of the most closed β-subunit with ATP ready for hydrolysis in the hydrolysis stroke of the F1 rotation | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a ATP hydrolysis | |
| 650 | 4 | |a Chemical shift analysis | |
| 650 | 4 | |a Conformation of ATP | |
| 650 | 4 | |a Conformational change of β-subunit | |
| 650 | 4 | |a Isotope-labeling | |
| 650 | 4 | |a Molecular motor | |
| 650 | 7 | |a Proton-Translocating ATPases |2 NLM | |
| 650 | 7 | |a EC 3.6.3.14 |2 NLM | |
| 650 | 7 | |a Adenosine Triphosphate |2 NLM | |
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| 700 | 1 | |a Miyasaka, Yoshiyuki |e verfasserin |4 aut | |
| 700 | 1 | |a Yagi, Hiromasa |e verfasserin |4 aut | |
| 700 | 1 | |a Kainosho, Masatsune |e verfasserin |4 aut | |
| 700 | 1 | |a Fujiwara, Toshimichi |e verfasserin |4 aut | |
| 700 | 1 | |a Akutsu, Hideo |e verfasserin |4 aut | |
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