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|Title:||Crosstalk along the stalk: Dynamics of the interaction of subunits B and F in the A1AO ATP synthase of methanosarcina mazei Gö1||Authors:||Grüber, G.
|Issue Date:||18-May-2010||Citation:||Grüber, G., Raghunathan, D., Gayen, S., Verma, C.S. (2010-05-18). Crosstalk along the stalk: Dynamics of the interaction of subunits B and F in the A1AO ATP synthase of methanosarcina mazei Gö1. Biochemistry 49 (19) : 4181-4190. ScholarBank@NUS Repository. https://doi.org/10.1021/bi9021236||Abstract:||The mechanism of coupling of ion pumping in the membrane-bound A O sector with ATP synthesis in the A3B3 headpiece of the A1 sector in the A1AO ATP synthase is a puzzle. Previously, crosstalk between the stalk and nucleotide-binding subunits FMm and BMm of the Methanosarcina mazei Gö1 A-ATP synthase has been observed by nucleotide-dependent cross-link formation of both subunits inside the enzyme. The recently determined NMR solution structure of FMm depicts the protein as a two-domain structure, with a well-folded N-terminus having 78 residues and a flexible C-terminal part (residues 79-101), proposed to become structured after binding to its partner, BMm. Here, we detail the crucial interactions between subunits BMm and FMm by determining the NMR structure of the very C-terminus of FMm, consisting of 20 residues and hereafter termed FMm(81-101), and performing molecular dynamics simulations on the resulting structure. These data demonstrate that the flexibility of the C-terminus enables FMm to switch between an elongated and retracted state. Docking and MD in conjunction with previously conducted and published NMR results, biochemical cross-linking, and fluorescence spectroscopy data were used to reconstruct a model of a B Mm-FMm assembly. The model of the BMm-F Mm complex shows the detailed interactions of helices 1 and 2 of the C-terminal domain of BMm with the C-terminal residues of F Mm. Movements of both helices of BMm accommodate the incoming C-terminus of FMm and connect the events of ion pumping and nucleotide binding in the A1AO ATP synthase. © 2010 American Chemical Society.||Source Title:||Biochemistry||URI:||http://scholarbank.nus.edu.sg/handle/10635/100355||ISSN:||00062960||DOI:||10.1021/bi9021236|
|Appears in Collections:||Staff Publications|
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