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

Authors :
Inga Pfeffer
Lennart Brewitz
Tobias Krojer
Sacha A. Jensen
Grazyna T. Kochan
Nadia J. Kershaw
Kirsty S. Hewitson
Luke A. McNeill
Holger Kramer
Martin Münzel
Richard J. Hopkinson
Udo Oppermann
Penny A. Handford
Michael A. McDonough
Christopher J. Schofield
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

Subjects :
Science

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