Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus.
The crystal structure of subunit F of vacuole-type ATPase/synthase (prokaryotic V-ATPase) was determined to of 2.2 A resolution. The subunit reveals unexpected structural similarity to the response regulator proteins that include the Escherichia coli chemotaxis response regulator CheY. The structure was successfully placed into the low-resolution EM structure of the prokaryotic holo-V-ATPase at a location indicated by the results of crosslinking experiments. The crystal structure, together with the single-molecule analysis using fluorescence resonance energy transfer, showed that the subunit F exhibits two conformations, a 'retracted' form in the absence and an 'extended' form in the presence of ATP. Our results postulated that the subunit F is a regulatory subunit in the V-ATPase.
Makyio
Hisayoshi
H
ATP System Project, Exploratory Research for Advanced Technology, Japan Science and Technology Agency, Yokohama, Japan.
Iino
Ryota
R
Ikeda
Chiyo
C
Imamura
Hiromi
H
Tamakoshi
Masatada
M
Iwata
Momi
M
Stock
Daniela
D
Bernal
Ricardo A
RA
Carpenter
Elisabeth P
EP
Yoshida
Masasuke
M
Yokoyama
Ken
K
Iwata
So
S
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D020035:Holoenzymes / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry* / Q000235:genetics; D016415:Sequence Alignment; D016963:Thermus thermophilus / Q000201:enzymology*; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics
D001426:Bacterial Proteins; D020035:Holoenzymes; D021122:Protein Subunits; D025262:Vacuolar Proton-Translocating ATPases