Abstract
F(1) is the water-soluble portion of the ubiquitous F(1)F(0) ATP synthase. Its structure includes three alpha- and three beta-subunits, arranged as a hexameric disc, plus a gamma-subunit that penetrates the center of the disc akin to an axle. Recently Hausrath et al. (Hausrath, A. C., Grüber, G., Matthews, B. W., and Capaldi, R. A. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 13697-13702) obtained an electron density map of E. coli F(1) at 4.4-A resolution in which the coiled-coil alpha-helices of the gamma-subunit could be seen to extend 45 A from the base of the alpha(3)beta(3) hexamer. Subsequently the structure of a truncated form of the E. coli gamma-subunit in complex with epsilon has been described (Rodgers, A. J. W., and Wilce, M. C. J. (2000) Nat. Struct. Biol. 7, 1051-1054). In the present study the 4.4-A resolution electron density map of E. coli F(1) is re-evaluated in light of the newly available data on the gamma- and epsilon-subunits. It is shown that the map of the F(1) complex is consistent with the structure of the isolated subunits. When E. coli F(1) is compared with that from beef heart, the structures of the E. coli gamma- and epsilon-subunits are seen to be generally similar to their counterparts in the bovine enzyme but to undergo major shifts in position. In particular, the two long, coiled-coil alpha-helices that lie along the axis of F(1) both unwind and rotate. Also the epsilon-subunit rotates around the axis by 81 degrees and undergoes a net translation of about 23 A. It is argued that these large-scale changes in conformation reflect distinct functional states that occur during the rotation of the gamma-subunit within the alpha(3)beta(3) hexamer.
Highlights
The F1F0 ATP synthase is an enzyme ubiquitous to bacteria, plants, and animals
In the present study the 4.4-Å resolution electron density map of E. coli F1 is re-evaluated in light of the newly available data on the ␥- and ⑀-subunits
Placement of the ␥- and ⑀-Subunits in the E. coli F1 Structure—The crystals of E. coli F1 used in the present analysis contain the ␣33 hexamer plus subunits ␥ and ⑀
Summary
The F1F0 ATP synthase is an enzyme ubiquitous to bacteria, plants, and animals. It utilizes a proton gradient across a membrane to drive the synthesis of ATP (1). Hausrath et al (7) obtained an electron density map of Escherichia coli F1 at 4.4-Å resolution in which the coiled-coil ␣-helices of the ␥-subunit could be seen to extend 45 Å from the base of the ␣33 hexamer. Other rod-like features in the electron density map were interpreted as additional ␣-helices of the ␥-subunit. The structure of a truncated form of the E. coli ␥-subunit (identified as ␥Ј) in complex with ⑀ has been described recently (9). This is consistent with some but not all aspects of the interpretation of Hausrath et al (7). Some rod-like features that were previously interpreted as ␣-helices are seen to correspond to regions of -sheet
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