Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase.
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.
Wilkens
S
S
Dunn
S D
SD
Chandler
J
J
Dahlquist
F W
FW
Capaldi
R A
RA
D003198:Computer Simulation; D004926:Escherichia coli / Q000201:enzymology*; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008961:Models, Structural; D010446:Peptide Fragments / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D012984:Software; D012996:Solutions
D046911:Macromolecular Substances; D010446:Peptide Fragments; D011994:Recombinant Proteins; D012996:Solutions; D006180:Proton-Translocating ATPases