Structural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes

The bacterial defense system McrBC is a two-component motor-driven nuclease complex that cleaves foreign DNA. Here, the authors present the structures of the GTP-specific AAA + motor protein McrB and two McrBC complexes and discuss the molecular mechanism of how McrC binding stimulates McrB GTP hydr...

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Autores principales:	Yiming Niu, Hiroshi Suzuki, Christopher J. Hosford, Thomas Walz, Joshua S. Chappie
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/69657620824b42129488ca2effba60cf
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id	oai:doaj.org-article:69657620824b42129488ca2effba60cf
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spelling	oai:doaj.org-article:69657620824b42129488ca2effba60cf2021-12-02T15:39:15ZStructural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes10.1038/s41467-020-19735-42041-1723https://doaj.org/article/69657620824b42129488ca2effba60cf2020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19735-4https://doaj.org/toc/2041-1723The bacterial defense system McrBC is a two-component motor-driven nuclease complex that cleaves foreign DNA. Here, the authors present the structures of the GTP-specific AAA + motor protein McrB and two McrBC complexes and discuss the molecular mechanism of how McrC binding stimulates McrB GTP hydrolysis.Yiming NiuHiroshi SuzukiChristopher J. HosfordThomas WalzJoshua S. ChappieNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-17 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yiming Niu Hiroshi Suzuki Christopher J. Hosford Thomas Walz Joshua S. Chappie Structural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes
description	The bacterial defense system McrBC is a two-component motor-driven nuclease complex that cleaves foreign DNA. Here, the authors present the structures of the GTP-specific AAA + motor protein McrB and two McrBC complexes and discuss the molecular mechanism of how McrC binding stimulates McrB GTP hydrolysis.
format	article
author	Yiming Niu Hiroshi Suzuki Christopher J. Hosford Thomas Walz Joshua S. Chappie
author_facet	Yiming Niu Hiroshi Suzuki Christopher J. Hosford Thomas Walz Joshua S. Chappie
author_sort	Yiming Niu
title	Structural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes
title_short	Structural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes
title_full	Structural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes
title_fullStr	Structural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes
title_full_unstemmed	Structural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes
title_sort	structural asymmetry governs the assembly and gtpase activity of mcrbc restriction complexes
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/69657620824b42129488ca2effba60cf
work_keys_str_mv	AT yimingniu structuralasymmetrygovernstheassemblyandgtpaseactivityofmcrbcrestrictioncomplexes AT hiroshisuzuki structuralasymmetrygovernstheassemblyandgtpaseactivityofmcrbcrestrictioncomplexes AT christopherjhosford structuralasymmetrygovernstheassemblyandgtpaseactivityofmcrbcrestrictioncomplexes AT thomaswalz structuralasymmetrygovernstheassemblyandgtpaseactivityofmcrbcrestrictioncomplexes AT joshuaschappie structuralasymmetrygovernstheassemblyandgtpaseactivityofmcrbcrestrictioncomplexes
_version_	1718385937485922304

Structural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes

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