Close examination of the bacterial flagellum motor and the ATPsynthase motor reveals many similarities, sufficient (say the authors) to â€œimply an evolutionary relation between the flagellum and F0F1-ATPsynthase and a similarity in the mechanism between FliI and F1-ATPase despite the apparently different functions of these proteinsâ€.
But is structural similarity a defining mark of an evolutionary relationship? On this basis, the octopus eye has to have an evolutionary relationship with the mammalian eye. Examples described as convergent evolution abound, and in these cases Darwinians invoke natural selection as the driver. Why is this not an option for molecular machines? The authors are so familiar with these complex systems that they know the absurdity of the convergence option: with parallel incremental changes under the influence of selection forces.
So, an â€œevolutionary relationshipâ€ is the only option â€“ or is it? Structural similarities due to intelligent design should also be evaluated as a hypothesis (but is rarely even considered as an option because naturalism is the dominant philosophy in science).
Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits
Katsumi Imada, Tohru Minamino, Aiko Tahara, and Keiichi Namba
Proc. Natl. Acad. Sci. USA, Published online before print January 3, 2007, doi: 10.1073/pnas.0608090104
Abstract: Construction of the bacterial flagellum in the cell exterior proceeds at its distal end by highly ordered self-assembly of many different component proteins, which are selectively exported through the central channel of the growing flagellum by the flagellar type III export apparatus. FliI is the ATPase of the export apparatus that drives the export process. Here we report the 2.4 Ã… resolution crystal structure of FliI in the ADP-bound form. FliI consists of three domains, and the whole structure shows extensive similarities to the α and β subunits of F0F1-ATPsynthase, a rotary motor that drives the chemical reaction of ATP synthesis. A hexamer model of FliI has been constructed based on the F1-ATPase structure composed of the α 3 β 3 γ subunits. Although the regions that differ in conformation between FliI and the F1- α / β subunits are all located on the outer surface of the hexamer ring, the main chain structures at the subunit interface and those surrounding the central channel of the ring are well conserved. These results imply an evolutionary relation between the flagellum and F0F1-ATPsynthase and a similarity in the mechanism between FliI and F1-ATPase despite the apparently different functions of these proteins.
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Evolution has become a favorite topic of the news media recently, but for some reason, they never seem to get the story straight. The staff at Discovery Institute's Center for Science and Culture started this Blog to set the record straight and make sure you knew "the rest of the story".
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We are a group of individuals, coming from diverse backgrounds and not speaking for any organization, who have found common ground around teleological concepts, including intelligent design. We think these concepts have real potential to generate insights about our reality that are being drowned out by political advocacy from both sides. We hope this blog will provide a small voice that helps rectify this situation.
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Complete zipped downloadable pdf copy of David Stove's devastating, and yet hard-to-find, critique of neo-Darwinism entitled "Darwinian Fairytales"
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