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NMR solution structure of subunit F of the methanogenic A1AO adenosine triphosphate synthase and its interaction with the nucleotide-binding subunit B

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NMR solution structure of subunit F of the methanogenic A1AO adenosine triphosphate synthase and its interaction with the nucleotide-binding subunit B

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dc.contributor.author Gayen, Shovanlal
dc.contributor.author Vivekanandan, Subramanian
dc.contributor.author Biuković, Goran
dc.contributor.author Grüber, Gerhard
dc.contributor.author Yoon, Ho Sup
dc.date.accessioned 2012-01-26T01:17:06Z
dc.date.available 2012-01-26T01:17:06Z
dc.date.copyright 2007
dc.date.issued 2012-01-26
dc.identifier.citation Gayen, S., Vivekanandan, S., Biuković, G., Grüber, G., & Yoon, H. S. (2007). NMR Solution Structure of Subunit F of the Methanogenic A1AO Adenosine Triphosphate Synthase and Its Interaction with the Nucleotide-Binding Subunit B. Biochemistry, 46(42), 11684-11694.
dc.identifier.uri http://hdl.handle.net/10220/7475
dc.description.abstract The A1AO adenosine triphosphate (ATP) synthase from archaea uses the ion gradients generated across the membrane sector (AO) to synthesize ATP in the A3B3 domain of the A1 sector. The energy coupling between the two active domains occurs via the so-called stalk part(s), to which the 12 kDa subunit F does belong. Here, we present the solution structure of the F subunit of the A1AO ATP synthase from Methanosarcina mazei Gö1. Subunit F exhibits a distinct two-domain structure, with the N-terminal having 78 residues and residues 79−101 forming the flexible C-terminal part. The well-ordered N-terminal domain is composed of a four-stranded parallel β-sheet structure and three α-helices placed alternately. The two domains are loosely associated with more flexibility relative to each other. The flexibility of the C-terminal domain is further confirmed by dynamics studies. In addition, the affinity of binding of mutant subunit F, with a substitution of Trp100 against Tyr and Ile at the very C-terminal end, to the nucleotide-binding subunit B was determined quantitatively using the fluorescence signals of natural subunit B (Trp430). Finally, the arrangement of subunit F within the complex is presented.
dc.language.iso en
dc.relation.ispartofseries Biochemistry
dc.rights © 2007 American Chemical Society.
dc.subject DRNTU::Science::Biological sciences
dc.title NMR solution structure of subunit F of the methanogenic A1AO adenosine triphosphate synthase and its interaction with the nucleotide-binding subunit B
dc.type Journal Article
dc.contributor.school School of Biological Sciences
dc.identifier.doi http://dx.doi.org/10.1021/bi701102n

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