Journal article
Comparative cross-linking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation
- Abstract:
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F-type ATPases are highly conserved enzymes used primarily for the synthesis of ATP. Here we apply mass spectrometry to the F1FO-ATPase, isolated from spinach chloroplasts, and uncover multiple modifications in soluble and membrane subunits. Mass spectra of the intact ATPase define a stable lipid ‘plug’ in the FO complex and reveal the stoichiometry of nucleotide binding in the F1 head. Comparing complexes formed in solution from an untreated ATPase with one incubated with a phosphatase revea...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 3.6MB, Terms of use)
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- Publisher copy:
- 10.1038/ncomms2985
Authors
Bibliographic Details
- Publisher:
- Springer Nature
- Journal:
- Nature Communications More from this journal
- Volume:
- 4
- Article number:
- 1985
- Publication date:
- 2013-06-12
- Acceptance date:
- 2013-05-07
- DOI:
- EISSN:
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2041-1723
Item Description
- Language:
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English
- Keywords:
- UUID:
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uuid:bd88d0c7-cca5-4587-b931-b7c8c0a1621d
- Local pid:
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pubs:401399
- Source identifiers:
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401399
- Deposit date:
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2013-11-17
Terms of use
- Copyright holder:
- Macmillan Publishers Limited
- Copyright date:
- 2013
- Notes:
- © 2013 Macmillan Publishers Limited. All rights reserved. This work is licensed under a Creative Commons Attribution 3.0 Unported License.
- Licence:
- CC Attribution (CC BY)
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