Journal article
Structures of PGAM5 provide insight into active site plasticity and multimeric assembly.
- Abstract:
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PGAM5 is a mitochondrial membrane protein that functions as an atypical Ser/Thr phosphatase and is a regulator of oxidative stress response, necroptosis, and autophagy. Here we present several crystal structures of PGAM5 including the activating N-terminal regulatory sequences, providing a model for structural plasticity, dimerization of the catalytic domain, and the assembly into an enzymatically active dodecameric form. Oligomeric states observed in structures were supported by hydrogen exc...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
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- Files:
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(pdf, 4.9MB)
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- Publisher copy:
- 10.1016/j.str.2017.05.020
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Authors
Funding
AbbVie
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Bayer Pharma AG
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Boehringer Ingelheim
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Canada Foundation for Innovation
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Bibliographic Details
- Publisher:
- Elsevier Publisher's website
- Journal:
- Structure Journal website
- Publication date:
- 2017-06-05
- Acceptance date:
- 2017-05-24
- DOI:
- EISSN:
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1878-4186
- ISSN:
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0969-2126
- Pubs id:
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pubs:702399
- URN:
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uri:fb44c9b5-211e-4d95-a026-9215d5de7f13
- UUID:
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uuid:fb44c9b5-211e-4d95-a026-9215d5de7f13
- Local pid:
- pubs:702399
Item Description
Terms of use
- Copyright holder:
- Knapp et al
- Copyright date:
- 2017
- Notes:
- © 2017 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
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