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Ion mobility-mass spectrometry of a rotary ATPase reveals ATP-induced reduction in conformational flexibility.

Abstract:

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 f...

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Publication status:
Published

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Publisher copy:
10.1038/nchem.1868

Authors


Politis, A More by this author
Davies, RB More by this author
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Journal:
Nature chemistry
Volume:
6
Issue:
3
Pages:
208-215
Publication date:
2014-03-05
DOI:
EISSN:
1755-4349
ISSN:
1755-4330
URN:
uuid:f35512c0-9c2c-4fa4-850b-041ce0b7f21f
Source identifiers:
449257
Local pid:
pubs:449257

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