- Abstract:
-
Vanadate is the hallmark inhibitor of the P-type ATPase family; however, structural details of its inhibitory mechanism have remained unresolved. We have determined the crystal structure of sarcoplasmic reticulum Ca(2+)-ATPase with bound vanadate in the absence of Ca(2+). Vanadate is bound at the catalytic site as a planar VO3(-) in complex with water and Mg(2+) in a dephosphorylation transition-state-like conformation. Validating bound VO3(-) by anomalous difference Fourier maps using long-w...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Accepted manuscript
- Files:
-
-
(pdf, 7.1MB)
-
- Publisher copy:
- 10.1016/j.str.2016.02.018
-
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- Publisher:
- Elsevier Ltd. Publisher's website
- Journal:
- Structure Journal website
- Volume:
- 24
- Issue:
- 4
- Pages:
- 617-623
- Publication date:
- 2016-04-05
- Acceptance date:
- 2016-02-25
- DOI:
- ISSN:
-
1878-4186 and 0969-2126
- Pubs id:
-
pubs:618919
- URN:
-
uri:9e389297-7d92-47f5-9731-f9a506c1b79b
- UUID:
-
uuid:9e389297-7d92-47f5-9731-f9a506c1b79b
- Local pid:
- pubs:618919
- Paper number:
- 4
- Language:
- English
- Keywords:
- Copyright holder:
- Elsevier Ltd.
- Copyright date:
- 2016
- Notes:
-
This is an
accepted manuscript of a journal article published by Elsevier in Structure on 2016-04-05, available online: http://dx.doi.org/10.1016/j.str.2016.02.018
Journal article
Crystal structure of the vanadate-inhibited Ca(2+)-ATPase
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