Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern
oleh: 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
| Format: | Article |
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| Diterbitkan: | Nature Portfolio 2019-10-01 |
Deskripsi
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.