Structure and subunit arrangement of the A-type ATP synthase complex from the archaeon Methanococcus jannaschii visualized by electron microscopy.
In Archaea, bacteria, and eukarya, ATP provides metabolic energy for energy-dependent processes. It is synthesized by enzymes known as A-type or F-type ATP synthase, which are the smallest rotatory engines in nature (Yoshida, M., Muneyuki, E., and Hisabori, T. (2001) Nat. Rev. Mol. Cell. Biol. 2, 669-677; Imamura, H., Nakano, M., Noji, H., Muneyuki, E., Ohkuma, S., Yoshida, M., and Yokoyama, K. (2003) Proc. Natl. Acad. Sci. U. S. A. 100, 2312-2315). Here, we report the first projected structure of an intact A(1)A(0) ATP synthase from Methanococcus jannaschii as determined by electron microscopy and single particle analysis at a resolution of 1.8 nm. The enzyme with an overall length of 25.9 nm is organized in an A(1) headpiece (9.4 x 11.5 nm) and a membrane domain, A(0) (6.4 x 10.6 nm), which are linked by a central stalk with a length of approximately 8 nm. A part of the central stalk is surrounded by a horizontal-situated rodlike structure ("collar"), which interacts with a peripheral stalk extending from the A(0) domain up to the top of the A(1) portion, and a second structure connecting the collar structure with A(1). Superposition of the three-dimensional reconstruction and the solution structure of the A(1) complex from Methanosarcina mazei Gö1 have allowed the projections to be interpreted as the A(1) headpiece, a central and the peripheral stalk, and the integral A(0) domain. Finally, the structural organization of the A(1)A(0) complex is discussed in terms of the structural relationship to the related motors, F(1)F(0) ATP synthase and V(1)V(0) ATPases.
Coskun
Unal
U
Universität des Saarlandes, Fachrichtung 2.5-Biophysik, D-66421 Homburg, Germany.
Chaban
Yuriy L
YL
Lingl
Astrid
A
Müller
Volker
V
Keegstra
Wilko
W
Boekema
Egbert J
EJ
Grüber
Gerhard
G
D025181:ATP Synthetase Complexes / Q000737:chemistry*; D000255:Adenosine Triphosphate / Q000737:chemistry; D001105:Archaea / Q000201:enzymology; D002499:Centrifugation, Density Gradient; D004591:Electrophoresis, Polyacrylamide Gel; D007091:Image Processing, Computer-Assisted; D017017:Methanococcus / Q000201:enzymology* / Q000648:ultrastructure; D008854:Microscopy, Electron; D008954:Models, Biological; D015999:Multivariate Analysis; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D006180:Proton-Translocating ATPases / Q000378:metabolism; D013329:Structure-Activity Relationship; D013395:Sucrose / Q000494:pharmacology
D013395:Sucrose; D000255:Adenosine Triphosphate; D025181:ATP Synthetase Complexes; D006180:Proton-Translocating ATPases