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
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/f7e2f575ff5740a38a278f59a178aaca
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spelling	oai:doaj.org-article:f7e2f575ff5740a38a278f59a178aaca2021-12-02T17:01:59ZAspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern10.1038/s41467-019-12711-72041-1723https://doaj.org/article/f7e2f575ff5740a38a278f59a178aaca2019-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-12711-7https://doaj.org/toc/2041-1723AspH 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.Inga PfefferLennart BrewitzTobias KrojerSacha A. JensenGrazyna T. KochanNadia J. KershawKirsty S. HewitsonLuke A. McNeillHolger KramerMartin MünzelRichard J. HopkinsonUdo OppermannPenny A. HandfordMichael A. McDonoughChristopher J. SchofieldNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-16 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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 Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern
description	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.
format	article
author	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
author_facet	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
author_sort	Inga Pfeffer
title	Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern
title_short	Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern
title_full	Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern
title_fullStr	Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern
title_full_unstemmed	Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern
title_sort	aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/f7e2f575ff5740a38a278f59a178aaca
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Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern

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