Rotary catalysis within ATP synthases: a bioinformatic approach provides novel insight into how large pH-dependent movements of the C-terminal helix of subunit c may be accommodated.
Hong
S
S
Department of Biological Chemistry, Johns Hopkins University, School of Medicine, 725 N. Wolfe Street, Baltimore, Maryland 21205-2185, USA.
Ko
Y H
YH
Pedersen
P L
PL
D025181:ATP Synthetase Complexes / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D020134:Catalytic Domain / Q000502:physiology*; D019295:Computational Biology / Q000379:methods; D017124:Conserved Sequence; D004926:Escherichia coli / Q000201:enzymology; D005057:Eukaryotic Cells / Q000201:enzymology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011387:Prokaryotic Cells / Q000201:enzymology; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D025181:ATP Synthetase Complexes