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Structural and Functional Features of the Escherichia coli F 1 -ATPase

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Abstract

The structural organization and overall dimensions of the Escherichia coli F1-ATPase in solutionhas been analyzed by synchroton X-ray scattering. Using an independent ab initio approach,the low-resolution shape of the hydrated enzyme was determined at 3.2 nm resolution. Theshape permitted unequivocal identification of the volume occupied by the α3 β3 γ complex ofthe atomic model of the ECF1-ATPase. The position of the ^σ and ∈ subunits were found byinteractive fitting of the solution scattering data and by cross-linking studies. Laser-inducedcovalent incorporation of 2-azido-ATP established a direct relationship between nucleotidebinding affinity and the different interactions between the stalk subunits γ and ∈ with the threecatalytic subunits (β) of the F1-ATPase. Mutants of the ECF1-ATPase with the introductionof Trp-for-Tyr replacement in the catalytic site of the complex made it possible to monitorthe activated state for ATP synthesis (ATP conformation) in which the γ and ∈ subunits arein close proximity to the α subunits and the ADP conformation, with the stalk subunits arelinked to the β subunit.

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  1. Fachbereich Biologie/Chemie, Abteilung Zoophysiologie, Universität Osnabrück, D-49069, Osnabrück, Germany

    Gerhard Grüber

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Grüber, G. Structural and Functional Features of the Escherichia coli F 1 -ATPase . J Bioenerg Biomembr 32, 341–346 (2000). https://doi.org/10.1023/A:1005519801891

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