Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase
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Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/nature10699.pdf
Reference41 articles.
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2. Toei, M. et al. Dodecamer rotor ring defines H+/ATP ratio for ATP synthesis of prokaryotic V-ATPase from Thermus thermophilus. Proc. Natl Acad. Sci. USA 104, 20256–20261 (2007)
3. Toei, M., Toei, S. & Forgac, M. Definition of membrane topology and identification of residues important for transport in subunit a of the vacuolar ATPase. J. Biol. Chem. 286, 35176–35186 (2011)
4. Numoto, N., Hasegawa, Y., Takeda, K. & Miki, K. Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase. EMBO Rep. 10, 1228–1234 (2009)
5. Lau, W. C. & Rubinstein, J. L. Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V(O) motor. Proc. Natl Acad. Sci. USA 107, 1367–1372 (2010)
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