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Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern
- Source :
- Nature Communications, Vol 10, Iss 1, Pp 1-16 (2019)
- Publication Year :
- 2019
- Publisher :
- Nature Portfolio, 2019.
-
Abstract
- AspH catalyses hydroxylation of asparagine and aspartate residues in epidermal growth factor-like domains (EGFDs). Here, the authors present crystal structures of AspH with and without substrates and show that AspH uses EFGD substrates with a non-canonical disulfide pattern.
- Subjects :
- Science
Subjects
Details
- Language :
- English
- ISSN :
- 20411723
- Volume :
- 10
- Issue :
- 1
- Database :
- Directory of Open Access Journals
- Journal :
- Nature Communications
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.f7e2f575ff5740a38a278f59a178aaca
- Document Type :
- article
- Full Text :
- https://doi.org/10.1038/s41467-019-12711-7