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

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

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.

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Autores principales: 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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Science
Q
Acceso en línea:https://doaj.org/article/f7e2f575ff5740a38a278f59a178aaca
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https://doaj.org/article/f7e2f575ff5740a38a278f59a178aaca

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