Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/104723
Title: Subunit F modulates ATP binding and migration in the nucleotide-binding subunit B of the A1AO ATP synthase of Methanosarcina mazei Gö1
Authors: Raghunathan, Devanathan
Gayen, Shovanlal
Kumar, Anil
Hunke, Cornelia
Grüber, Gerhard
Verma, Chandra S.
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2012
Source: Raghunathan, D., Gayen, S., Kumar, A., Hunke, C., Grüber, G., & Verma, C. S. (2012). 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), 213-224.
Series/Report no.: Journal of bioenergetics and biomembranes
Abstract: The interaction of the nucleotide-binding subunit B with subunit F is essential in coupling of ion pumping and ATP synthesis in A1AO 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 A1AO 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.
URI: https://hdl.handle.net/10356/104723
http://hdl.handle.net/10220/17008
ISSN: 0145-479X
DOI: 10.1007/s10863-012-9410-y
Schools: School of Biological Sciences 
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SBS Journal Articles

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