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Structures of PGAM5 provide insight into active site plasticity and multimeric assembly.

Abstract:

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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Publisher copy:
10.1016/j.str.2017.05.020

Authors


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Department:
Oxford, MSD, NDM, Structural Genomics Consortium
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Department:
Oxford, MSD, NDM, Structural Genomics Consortium
Marcsisin, SR More by this author
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Department:
Oxford, MSD, NDM, Structural Genomics Consortium
Schröder, M More by this author
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Bayer Pharma AG More from this funder
Boehringer Ingelheim More from this funder
Canada Foundation for Innovation More from this funder
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Publisher:
Elsevier Publisher's website
Journal:
Structure Journal website
Publication date:
2017-06-05
Acceptance date:
2017-05-24
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
Pubs id:
pubs:702399
URN:
uri:fb44c9b5-211e-4d95-a026-9215d5de7f13
UUID:
uuid:fb44c9b5-211e-4d95-a026-9215d5de7f13
Local pid:
pubs:702399

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