Small-Angle X-ray Scattering Reveals the Solution Structure of the Peripheral Stalk Subunit H of the A1AO ATP Synthase from Methanocaldococcus jannaschii and Its Binding to the Catalytic A Subunit
Author:
Affiliation:
1. School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, and European Molecular Biology Laboratory, Hamburg Outstation, EMBL c/o DESY, D-22603 Hamburg, Germany
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi062123n
Reference48 articles.
1. Bioenergetics of the Archaea
2. Structure and Mechanism of Vacuolar Na+-Translocating ATPase From Enterococcus hirae
3. The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio
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1. Random-Coil Behavior of Chemically Denatured Topologically Knotted Proteins Revealed by Small-Angle X-ray Scattering;The Journal of Physical Chemistry B;2015-04-21
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 divergence of the rotary ATPases;Quarterly Reviews of Biophysics;2011-03-22
4. Subunit–subunit interactions and overall topology of the dimeric mitochondrial ATP synthase of Polytomella sp.;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2010-08
5. 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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