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Title: Subunit F modulates ATP binding and migration in the nucleotide-binding subunit B of the A 1A O ATP synthase of Methanosarcina mazei Gö1
Authors: Raghunathan, D.
Gayen, S.
Kumar, A.
Hunke, C.
Grüber, G.
Verma, C.S. 
Keywords: A 1A O ATP synthase
Fluorescence correlation spectroscopy (FCS)
Isothermal titration calorimetry (ITC)
Molecular dynamics simulations
Nuclear magnetic resonance (NMR)
Subunit B
Issue Date: Feb-2012
Citation: Raghunathan, D., Gayen, S., Kumar, A., Hunke, C., Grüber, G., Verma, C.S. (2012-02). Subunit F modulates ATP binding and migration in the nucleotide-binding subunit B of the A 1A O ATP synthase of Methanosarcina mazei Gö1. Journal of Bioenergetics and Biomembranes 44 (1) : 213-224. ScholarBank@NUS Repository.
Abstract: The interaction of the nucleotide-binding subunit B with subunit F is essential in coupling of ion pumping and ATP synthesis in A 1A O ATP synthases. Here we provide structural and thermodynamic insights on the nucleotide binding to the surface of subunits B and F of Methanosarcina mazei Gö1 A 1A O ATP synthase, which initiated migration to its final binding pocket via two transitional intermediates on the surface of subunit B. NMR- and fluorescence spectroscopy as well as ITC data combined with molecular dynamics simulations of the nucleotide bound subunit B and nucleotide bound B-F complex in explicit solvent, suggests that subunit F is critical for the migration to and eventual occupancy of the final binding site by the nucleotide of subunit B. Rotation of the C-terminus and conformational changes in subunit B are initiated upon binding with subunit F causing a perturbation that leads to the migration of ATP from the transition site 1 through an intermediate transition site 2 to the final binding site 3. This mechanism is elucidated on the basis of change in binding affinity for the nucleotide at the specific sites on subunit B upon complexation with subunit F. The change in enthalpy is further explained based on the fluctuating local environment around the binding sites. © 2012 Springer Science+Business Media, LLC.
Source Title: Journal of Bioenergetics and Biomembranes
ISSN: 0145479X
DOI: 10.1007/s10863-012-9410-y
Appears in Collections:Staff Publications

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