Subunit F modulates ATP binding and migration in the nucleotide-binding subunit B of the A[subscript 1]A[subscript O] ATP synthase of Methanosarcina mazei Gö1
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Author(s)
Raghunathan, Devanathan
Gayen, Shovanlal
Kumar, Anil
Hunke, Cornelia
Grüber, Gerhard
Verma, Chandra S.
Alternative Title
Subunit F modulates ATP binding and migration in the nucleotide-binding subunit B of the A1AO ATP synthase of Methanosarcina mazei Gö1
Date Issued
February 2012
Journal
Journal of Bioenergetics and Biomembranes
Publisher
Springer US
Citation
Raghunathan, Devanathan et al. “Subunit F Modulates ATP Binding and Migration in the Nucleotide-Binding Subunit B of the A1AO ATP Synthase of Methanosarcina Mazei Gö1.” Journal of Bioenergetics and Biomembranes 44.1 (2012): 213–224.
Version
Author's final manuscript
Abstract
The interaction of the nucleotide-binding subunit B with subunit F is essential in coupling of ion pumping and ATP synthesis in A[subscript 1]A[subscript 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[subscript 1]A[subscript 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.
MIT Department
Singapore-MIT Alliance in Research and Technology (SMART)
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DOI of Published Version
https://doi.org/10.1007/s10863-012-9410-y
