Journal
NATURE CHEMISTRY
Volume 6, Issue 3, Pages 208-215Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEM.1868
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Funding
- Wellcome Trust
- PROSPECTS within the Research Framework of the European Union [HEALTHF4-2008-201648]
- Engineering and Physical Sciences Research Council
- Royal Society
- European Research Council
- Australian National Health and Medical Research Council [1004620, 1022143, 1047004]
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Rotary ATPases play fundamental roles in energy conversion as their catalytic rotation is associated with interdomain fluctuations and heterogeneity of conformational states. Using ion mobility mass spectrometry we compared the conformational dynamics of the intact ATPase from Thermus thermophilus with those of its membrane and soluble subcomplexes. Our results define regions with enhanced flexibility assigned to distinct subunits within the overall assembly. To provide a structural context for our experimental data we performed molecular dynamics simulations and observed conformational changes of the peripheral stalks that reflect their intrinsic flexibility. By isolating complexes at different phases of cell growth and manipulating nucleotides, metal ions and pH during isolation, we reveal differences that can be related to conformational changes in the V-o complex triggered by ATP binding. Together these results implicate nucleotides in modulating flexibility of the stator components and uncover mechanistic detail that underlies operation and regulation in the context of the holoenzyme.
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