NMR solution structure of the N-terminal domain of subunit E (E1–52) of A1AO ATP synthase from Methanocaldococcus jannaschii
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Physiology
Link
http://link.springer.com/content/pdf/10.1007/s10863-009-9237-3.pdf
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1. The Structure of Subunit E of the Pyrococcus horikoshii OT3 A-ATP Synthase Gives Insight into the Elasticity of the Peripheral Stalk;Journal of Molecular Biology;2012-07
2. Binding of subunit E into the A–B interface of the A1AO ATP synthase;Biochimica et Biophysica Acta (BBA) - Biomembranes;2011-09
3. Structural elements of the C-terminal domain of subunit E (E133-222) from the Saccharomyces cerevisiae V1VO ATPase determined by solution NMR spectroscopy;Journal of Bioenergetics and Biomembranes;2011-08-09
4. Crystal and solution structure of the C-terminal part of the Methanocaldococcus jannaschii A1AO ATP synthase subunit E revealed by X-ray diffraction and small-angle X-ray scattering;Journal of Bioenergetics and Biomembranes;2010-06-23
5. A site-directed cross-linking approach to the characterization of subunit E-subunit G contacts in the vacuolar H+-ATPase stator;Molecular Membrane Biology;2010-05-06
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