Disulfide linkage in the coiled-coil domain of subunit H of A1 AO ATP synthase from Methanocaldococcus jannaschii and the NMR structure of the C-terminal segment H85-104
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/j.febslet.2009.12.024/fullpdf
Reference28 articles.
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2. New insights into structure-function relationships between archeal ATP synthase (A1AO) and vacuolar type ATPase (V1VO);Grüber;BioEssays,2008
3. Three-dimensional structure of A1AO ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy;Vonck;J. Biol. Chem.,2009
4. Structure and subunit arrangement of the A-type ATP synthase complex from the archaeon Methanocaldococcus jannaschii visualized by electron microscopy;Coskun;J. Biol. Chem.,2004
5. Three-dimensional structure of the intact Thermus thermophilus H+-ATPase/synthase by electron microscopy;Bernal;Structure,2004
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. ACCORD: an assessment tool to determine the orientation of homodimeric coiled-coils;Scientific Reports;2017-03-07
2. 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
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