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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

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Journal:
Nature chemistry More from this journal
Volume:
6
Issue:
3
Pages:
208-215
Publication date:
2014-03-01
DOI:
EISSN:
1755-4349
ISSN:
1755-4330
Language:
English
Keywords:
Pubs id:
pubs:449257
UUID:
uuid:f35512c0-9c2c-4fa4-850b-041ce0b7f21f
Local pid:
pubs:449257
Source identifiers:
449257
Deposit date:
2014-02-24

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