Solution structure of the N-terminal domain of the δ subunit of the E. coli ATPsynthase
- 1 March 1997
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 4 (3) , 198-201
- https://doi.org/10.1038/nsb0397-198
Abstract
NMR studies of the delta subunit of the Escherichia coli F1F0-ATPsynthase reveal that it consists of an N-terminal six alpha-helix bundle and a less well ordered C terminus. Both domains are part of one of two separate connections between F1 and F0.Keywords
This publication has 34 references indexed in Scilit:
- Oligomycin Sensitivity Conferring Protein of Mitochondrial ATP Synthase: Deletions in the N-Terminal End Cause Defects in Interactions with F1, while Deletions in the C-Terminal End Cause Defects in Interactions with FoBiochemistry, 1996
- Christian B. AnfinsenNature Structural & Molecular Biology, 1995
- Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondriaNature, 1994
- Escherichia coli H+-ATPase: Role of the δ subunit in binding F1 to the F0 sectorArchives of Biochemistry and Biophysics, 1992
- Structure-function relationships of domains of the δ subunit in Escherichia coli adenosine triphosphataseBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1991
- Structure of the ATP synthase complex (ECF1F0) of Escherichia coli from cryoelectron microscopyBiochemistry, 1990
- ATP SYNTHASE (H+-ATPase): Results by Combined Biochemical and Molecular Biological ApproachesAnnual Review of Biochemistry, 1989
- ATP synthesis by oxidative phosphorylationPhysiological Reviews, 1988
- Amino acid sequence of the oligomycin sensitivity‐conferring protein (OSCP) of beef‐heart mitochondria and its homology with the δ‐subunit of the F1‐ATPase of Escherichia coliFEBS Letters, 1984
- A MACROMOLECULAR REPEATING UNIT OF MITOCHONDRIAL STRUCTURE AND FUNCTIONThe Journal of cell biology, 1964