Structure of a full-length bacterial polysaccharide co-polymerase

Lipopolysaccharides, important components of the bacterial cell envelope, are synthesized at the inner membrane by the Wzx/Wzy-dependent assembly pathway. A cryo-EM structure of an intact E. coli WzzB, the polysaccharide co-polymerase component of this pathway, reveals details of the transmembrane,...

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Autores principales:	Benjamin Wiseman, Ram Gopal Nitharwal, Göran Widmalm, Martin Högbom
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/1ee44a4ef17c4cc6a456eb3b1384aa08
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spelling	oai:doaj.org-article:1ee44a4ef17c4cc6a456eb3b1384aa082021-12-02T14:12:05ZStructure of a full-length bacterial polysaccharide co-polymerase10.1038/s41467-020-20579-12041-1723https://doaj.org/article/1ee44a4ef17c4cc6a456eb3b1384aa082021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20579-1https://doaj.org/toc/2041-1723Lipopolysaccharides, important components of the bacterial cell envelope, are synthesized at the inner membrane by the Wzx/Wzy-dependent assembly pathway. A cryo-EM structure of an intact E. coli WzzB, the polysaccharide co-polymerase component of this pathway, reveals details of the transmembrane, cytoplasmic domains and a conserved a proline-rich segment proximal to the C-terminal transmembrane helix.Benjamin WisemanRam Gopal NitharwalGöran WidmalmMartin HögbomNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Benjamin Wiseman Ram Gopal Nitharwal Göran Widmalm Martin Högbom Structure of a full-length bacterial polysaccharide co-polymerase
description	Lipopolysaccharides, important components of the bacterial cell envelope, are synthesized at the inner membrane by the Wzx/Wzy-dependent assembly pathway. A cryo-EM structure of an intact E. coli WzzB, the polysaccharide co-polymerase component of this pathway, reveals details of the transmembrane, cytoplasmic domains and a conserved a proline-rich segment proximal to the C-terminal transmembrane helix.
format	article
author	Benjamin Wiseman Ram Gopal Nitharwal Göran Widmalm Martin Högbom
author_facet	Benjamin Wiseman Ram Gopal Nitharwal Göran Widmalm Martin Högbom
author_sort	Benjamin Wiseman
title	Structure of a full-length bacterial polysaccharide co-polymerase
title_short	Structure of a full-length bacterial polysaccharide co-polymerase
title_full	Structure of a full-length bacterial polysaccharide co-polymerase
title_fullStr	Structure of a full-length bacterial polysaccharide co-polymerase
title_full_unstemmed	Structure of a full-length bacterial polysaccharide co-polymerase
title_sort	structure of a full-length bacterial polysaccharide co-polymerase
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/1ee44a4ef17c4cc6a456eb3b1384aa08
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Structure of a full-length bacterial polysaccharide co-polymerase

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