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Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern

Abstract:

AspH is an endoplasmic reticulum (ER) membrane-anchored 2-oxoglutarate oxygenase whose C-terminal oxygenase and tetratricopeptide repeat (TPR) domains present in the ER lumen. AspH catalyses hydroxylation of asparaginyl- and aspartyl-residues in epidermal growth factor-like domains (EGFDs). Here we report crystal structures of human AspH, with and without substrate, that reveal substantial conformational changes of the oxygenase and TPR domains during substrate binding. Fe(II)-binding by AspH...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41467-019-12711-7

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
ORCID:
0000-0003-0661-0814
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Role:
Author
ORCID:
0000-0002-0560-9531
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Publisher:
Nature Research Publisher's website
Journal:
Nature Communications Journal website
Volume:
10
Article number:
4910
Publication date:
2019-10-28
Acceptance date:
2019-09-26
DOI:
ISSN:
2041-1723
Source identifiers:
1068525
Language:
English
Keywords:
Pubs id:
pubs:1068525
UUID:
uuid:0a1194dd-a9fc-4cd5-9390-46c2c68e9f33
Local pid:
pubs:1068525
Deposit date:
2019-10-30

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