Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action

Sialidases are glycoside hydrolases that cleave sialosides. Here the authors define the 3-D structure, alone and in complex with products and inhibitors, of the CAZy family GH156 sialidase, EnvSia156, showing it displays a catalytical (β/α) 8-barrel domain distinct from other sialidases and allowing...

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Autores principales:	Pedro Bule, Léa Chuzel, Elena Blagova, Liang Wu, Melissa A. Gray, Bernard Henrissat, Erdmann Rapp, Carolyn R. Bertozzi, Christopher H. Taron, Gideon J. Davies
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/0c2efbe0238a4ca8b32604be548a3735
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spelling	oai:doaj.org-article:0c2efbe0238a4ca8b32604be548a37352021-12-02T14:39:41ZInverting family GH156 sialidases define an unusual catalytic motif for glycosidase action10.1038/s41467-019-12684-72041-1723https://doaj.org/article/0c2efbe0238a4ca8b32604be548a37352019-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-12684-7https://doaj.org/toc/2041-1723Sialidases are glycoside hydrolases that cleave sialosides. Here the authors define the 3-D structure, alone and in complex with products and inhibitors, of the CAZy family GH156 sialidase, EnvSia156, showing it displays a catalytical (β/α) 8-barrel domain distinct from other sialidases and allowing description of its inverting catalytic mechanism.Pedro BuleLéa ChuzelElena BlagovaLiang WuMelissa A. GrayBernard HenrissatErdmann RappCarolyn R. BertozziChristopher H. TaronGideon J. DaviesNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Pedro Bule Léa Chuzel Elena Blagova Liang Wu Melissa A. Gray Bernard Henrissat Erdmann Rapp Carolyn R. Bertozzi Christopher H. Taron Gideon J. Davies Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action
description	Sialidases are glycoside hydrolases that cleave sialosides. Here the authors define the 3-D structure, alone and in complex with products and inhibitors, of the CAZy family GH156 sialidase, EnvSia156, showing it displays a catalytical (β/α) 8-barrel domain distinct from other sialidases and allowing description of its inverting catalytic mechanism.
format	article
author	Pedro Bule Léa Chuzel Elena Blagova Liang Wu Melissa A. Gray Bernard Henrissat Erdmann Rapp Carolyn R. Bertozzi Christopher H. Taron Gideon J. Davies
author_facet	Pedro Bule Léa Chuzel Elena Blagova Liang Wu Melissa A. Gray Bernard Henrissat Erdmann Rapp Carolyn R. Bertozzi Christopher H. Taron Gideon J. Davies
author_sort	Pedro Bule
title	Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action
title_short	Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action
title_full	Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action
title_fullStr	Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action
title_full_unstemmed	Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action
title_sort	inverting family gh156 sialidases define an unusual catalytic motif for glycosidase action
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/0c2efbe0238a4ca8b32604be548a3735
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Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action

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