Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein

In type I-D CRISPR–Cas systems, the nuclease and helicase activities are carried out by separate subunits. The crystal structure of Sulfolobus islandicus type I-D large subunit Cas10d, containing a nuclease domain, reveals unusual architecture. The structure of Cas10d in complex with anti-CRISPR pro...

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Autores principales:	M. Cemre Manav, Lan B. Van, Jinzhong Lin, Anders Fuglsang, Xu Peng, Ditlev E. Brodersen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/8bfbe88217324a9380cd181e40d561c4
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spelling	oai:doaj.org-article:8bfbe88217324a9380cd181e40d561c42021-12-02T13:57:22ZStructural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein10.1038/s41467-020-19847-x2041-1723https://doaj.org/article/8bfbe88217324a9380cd181e40d561c42020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19847-xhttps://doaj.org/toc/2041-1723In type I-D CRISPR–Cas systems, the nuclease and helicase activities are carried out by separate subunits. The crystal structure of Sulfolobus islandicus type I-D large subunit Cas10d, containing a nuclease domain, reveals unusual architecture. The structure of Cas10d in complex with anti-CRISPR protein AcrID1 suggests that the latter sequesters Cas10d in a nonfunctional state.M. Cemre ManavLan B. VanJinzhong LinAnders FuglsangXu PengDitlev E. BrodersenNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q M. Cemre Manav Lan B. Van Jinzhong Lin Anders Fuglsang Xu Peng Ditlev E. Brodersen Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein
description	In type I-D CRISPR–Cas systems, the nuclease and helicase activities are carried out by separate subunits. The crystal structure of Sulfolobus islandicus type I-D large subunit Cas10d, containing a nuclease domain, reveals unusual architecture. The structure of Cas10d in complex with anti-CRISPR protein AcrID1 suggests that the latter sequesters Cas10d in a nonfunctional state.
format	article
author	M. Cemre Manav Lan B. Van Jinzhong Lin Anders Fuglsang Xu Peng Ditlev E. Brodersen
author_facet	M. Cemre Manav Lan B. Van Jinzhong Lin Anders Fuglsang Xu Peng Ditlev E. Brodersen
author_sort	M. Cemre Manav
title	Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein
title_short	Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein
title_full	Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein
title_fullStr	Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein
title_full_unstemmed	Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein
title_sort	structural basis for inhibition of an archaeal crispr–cas type i-d large subunit by an anti-crispr protein
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/8bfbe88217324a9380cd181e40d561c4
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Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein

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