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Structural basis of unisite catalysis of bacterial F 0 F 1 -ATPase.

التفاصيل البيبلوغرافية
العنوان: Structural basis of unisite catalysis of bacterial F 0 F 1 -ATPase.
المؤلفون: Nakano A; Department of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kita-ku, Kyoto 603-8555, Japan., Kishikawa JI; Department of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kita-ku, Kyoto 603-8555, Japan.; Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan., Nakanishi A; Department of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kita-ku, Kyoto 603-8555, Japan.; Research Center for Ultra-High Voltage Electron Microscopy, Osaka University, 7-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan., Mitsuoka K; Research Center for Ultra-High Voltage Electron Microscopy, Osaka University, 7-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan., Yokoyama K; Department of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kita-ku, Kyoto 603-8555, Japan.
المصدر: PNAS nexus [PNAS Nexus] 2022 Jul 11; Vol. 1 (3), pp. pgac116. Date of Electronic Publication: 2022 Jul 11 (Print Publication: 2022).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Oxford University Press on behalf of the National Academy of Sciences Country of Publication: England NLM ID: 9918367777906676 Publication Model: eCollection Cited Medium: Internet ISSN: 2752-6542 (Electronic) Linking ISSN: 27526542 NLM ISO Abbreviation: PNAS Nexus Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: [Oxford] : Oxford University Press on behalf of the National Academy of Sciences, [2022]-
مستخلص: Adenosine triphosphate (ATP) synthases (F 0 F 1 -ATPases) are crucial for all aerobic organisms. F 1 , a water-soluble domain, can catalyze both the synthesis and hydrolysis of ATP with the rotation of the central γε rotor inside a cylinder made of α 3 β 3 in three different conformations (referred to as β E , β TP , and β DP ). In this study, we determined multiple cryo-electron microscopy structures of bacterial F 0 F 1 exposed to different reaction conditions. The structures of nucleotide-depleted F 0 F 1 indicate that the ε subunit directly forces β TP to adopt a closed form independent of the nucleotide binding to β TP . The structure of F 0 F 1 under conditions that permit only a single catalytic β subunit per enzyme to bind ATP is referred to as unisite catalysis and reveals that ATP hydrolysis unexpectedly occurs on β TP instead of β DP , where ATP hydrolysis proceeds in the steady-state catalysis of F 0 F 1 . This indicates that the unisite catalysis of bacterial F 0 F 1 significantly differs from the kinetics of steady-state turnover with continuous rotation of the shaft.
(© The Author(s) 2022. Published by Oxford University Press on behalf of National Academy of Sciences.)
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تواريخ الأحداث: Date Created: 20230206 Latest Revision: 20230207
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC9896953
DOI: 10.1093/pnasnexus/pgac116
PMID: 36741449
قاعدة البيانات: MEDLINE
الوصف
تدمد:2752-6542
DOI:10.1093/pnasnexus/pgac116