Ion mobility–mass spectrometry of a rotary ATPase reveals ATP-induced reduction in conformational flexibility-Reference-Cited by-同舟云学术

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Ion mobility–mass spectrometry of a rotary ATPase reveals ATP-induced reduction in conformational flexibility

Published:2014-02-16 Issue:3 Volume:6 Page:208-215
ISSN:1755-4330
Container-title:Nature Chemistry
language:en
Short-container-title:Nature Chem

Author:

Zhou Min,Politis Argyris,Davies Roberta B.,Liko Idlir,Wu Kuan-Jung,Stewart Alastair G.,Stock Daniela,Robinson Carol V.

Publisher

Springer Science and Business Media LLC

Subject

General Chemical Engineering,General Chemistry

Link

http://www.nature.com/articles/nchem.1868.pdf

Reference48 articles.

1. von Ballmoos, C., Cook, G. M. & Dimroth, P. Unique rotary ATP synthase and its biological diversity. Annu. Rev. Biophys. 37, 43–64 (2008).

2. Stewart, A. G., Sobti, M., Harvey, R. P. & Stock, D. Rotary ATPases: models, machine elements and technical specifications. Bioarchitecture 3, 2–12 (2013).

3. Nakano, M. et al. ATP hydrolysis and synthesis of a rotary motor V-ATPase from Thermus thermophilus. J. Biol. Chem. 283, 20789–20796 (2008).

4. Feniouk, B. A., Suzuki, T & Yoshida, M. Regulatory interplay between proton motive force, ADP, phosphate, and subunit epsilon in bacterial ATP synthase. J. Biol. Chem. 282, 764–772 (2007).

5. Muench, S. P., Trinick, J. & Harrison, M. A. Structural divergence of the rotary ATPases. Q. Rev. Biophys. 44, 311–356 (2011).

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