Arginine-induced conformational change in the c-ring/ a-subunit interface of ATP synthase

Vorburger, Thomas; Ebneter, Judith Zingg; Wiedenmann, Alexander; Morger, Damien; Weber, Gerald; Diederichs, Kay; Dimroth, Peter; Ballmoos, Christoph von

Arginine-induced conformational change in the c-ring/ a-subunit interface of ATP synthase

Dateien

Diederichs opus-119534.pdfGröße: 6.88 MBDownloads: 574

Datum

2008

Autor:innen

Vorburger, Thomas

Ebneter, Judith Zingg

Wiedenmann, Alexander

Morger, Damien

Weber, Gerald

Diederichs, Kay

Dimroth, Peter

Ballmoos, Christoph von

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

The FEBS journal. 2008, 275(9), pp. 2137-2150. ISSN 1742-464X. eISSN 1742-4658. Available under: doi: 10.1111/j.1742-4658.2008.06368.x

Zusammenfassung

The rotational mechanism of ATP synthases requires a unique interface between the stator a subunit and the rotating c-ring to accommodate stability and smooth rotation simultaneously. The recently published c-ring crystal structure of the ATP synthase of Ilyobacter tartaricus represents the conformation in the absence of subunit a. However, in order to understand the dynamic structural processes during ion translocation, studies in the presence of subunit a are required. Here, by intersubunit Cys-Cys cross-linking, the relative topography of the interacting helical faces of subunits a and c from the I. tartaricus ATP synthase has been mapped. According to these data, the essential stator arginine (aR226) is located between the c-ring binding pocket and the cytoplasm. Furthermore, the spatially vicinal residues cT67C and cG68C in the isolated c-ring structure yielded largely asymmetric cross-linking products with aN230C of subunit a, suggesting a small, but significant conformational change of binding-site residues upon contact with subunit a. The conformational change was dependent on the positive charge of the stator arginine or the aR226H substitution. Energy-minimization calculations revealed possible modes for the interaction between the stator arginine and the c-ring. These biochemical results and structural restraints support a model in which the stator arginine operates as a pendulum, moving in and out of the binding pocket as the c-ring rotates along the interface with subunit a. This mechanism allows efficient interaction between subunit a and the c-ring and simultaneously allows almost frictionless movement against each other.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Schlagwörter

a/c interface, ATP synthase, c-ring, cysteine cross-linking, ion-binding pocket

Zitieren

ISO 690

VORBURGER, Thomas, Judith Zingg EBNETER, Alexander WIEDENMANN, Damien MORGER, Gerald WEBER, Kay DIEDERICHS, Peter DIMROTH, Christoph von BALLMOOS, 2008. Arginine-induced conformational change in the c-ring/ a-subunit interface of ATP synthase. In: The FEBS journal. 2008, 275(9), pp. 2137-2150. ISSN 1742-464X. eISSN 1742-4658. Available under: doi: 10.1111/j.1742-4658.2008.06368.x

BibTex

@article{Vorburger2008Argin-1234,
  year={2008},
  doi={10.1111/j.1742-4658.2008.06368.x},
  title={Arginine-induced conformational change in the c-ring/ a-subunit interface of ATP synthase},
  number={9},
  volume={275},
  issn={1742-464X},
  journal={The FEBS journal},
  pages={2137--2150},
  author={Vorburger, Thomas and Ebneter, Judith Zingg and Wiedenmann, Alexander and Morger, Damien and Weber, Gerald and Diederichs, Kay and Dimroth, Peter and Ballmoos, Christoph von}
}

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Universitätsbibliographie

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