Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC

McrBC is a bacterial antiphage defense system that cleaves methylated DNA and is composed of the AAA+ GTPase motor McrB and the endonuclease McrC. Here, the authors present the cryo-EM structure of E. coli McrBC that reveals how McrC inserts a stalk-like structure into the pore of the ring-shaped Mc...

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Autores principales:	Neha Nirwan, Yuzuru Itoh, Pratima Singh, Sutirtha Bandyopadhyay, Kutti R. Vinothkumar, Alexey Amunts, Kayarat Saikrishnan
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5c68680d22bd42158914fb12b267b2bd
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spelling	oai:doaj.org-article:5c68680d22bd42158914fb12b267b2bd2021-12-02T15:36:02ZStructure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC10.1038/s41467-019-11084-12041-1723https://doaj.org/article/5c68680d22bd42158914fb12b267b2bd2019-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11084-1https://doaj.org/toc/2041-1723McrBC is a bacterial antiphage defense system that cleaves methylated DNA and is composed of the AAA+ GTPase motor McrB and the endonuclease McrC. Here, the authors present the cryo-EM structure of E. coli McrBC that reveals how McrC inserts a stalk-like structure into the pore of the ring-shaped McrB hexamer and discuss mechanistic implications.Neha NirwanYuzuru ItohPratima SinghSutirtha BandyopadhyayKutti R. VinothkumarAlexey AmuntsKayarat SaikrishnanNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-9 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Neha Nirwan Yuzuru Itoh Pratima Singh Sutirtha Bandyopadhyay Kutti R. Vinothkumar Alexey Amunts Kayarat Saikrishnan Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC
description	McrBC is a bacterial antiphage defense system that cleaves methylated DNA and is composed of the AAA+ GTPase motor McrB and the endonuclease McrC. Here, the authors present the cryo-EM structure of E. coli McrBC that reveals how McrC inserts a stalk-like structure into the pore of the ring-shaped McrB hexamer and discuss mechanistic implications.
format	article
author	Neha Nirwan Yuzuru Itoh Pratima Singh Sutirtha Bandyopadhyay Kutti R. Vinothkumar Alexey Amunts Kayarat Saikrishnan
author_facet	Neha Nirwan Yuzuru Itoh Pratima Singh Sutirtha Bandyopadhyay Kutti R. Vinothkumar Alexey Amunts Kayarat Saikrishnan
author_sort	Neha Nirwan
title	Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC
title_short	Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC
title_full	Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC
title_fullStr	Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC
title_full_unstemmed	Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC
title_sort	structure-based mechanism for activation of the aaa+ gtpase mcrb by the endonuclease mcrc
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/5c68680d22bd42158914fb12b267b2bd
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Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC

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