A substrate binding model for the KEOPS tRNA modifying complex

KEOPS is an evolutionary conserved complex with a core of four core subunits—Pcc1, Kae1, Bud32 and Cgi121—that catalyzes the universal and essential tRNA modification N6-threonylcarbamoyl adenosine (t6A). Here the authors describe a Cgi121-tRNA crystal structure and new composite model of the KEOPS...

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Autores principales:	Jonah Beenstock, Samara Mishelle Ona, Jennifer Porat, Stephen Orlicky, Leo C. K. Wan, Derek F. Ceccarelli, Pierre Maisonneuve, Rachel K. Szilard, Zhe Yin, Dheva Setiaputra, Daniel Y. L. Mao, Morgan Khan, Shaunak Raval, David C. Schriemer, Mark A. Bayfield, Daniel Durocher, Frank Sicheri
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/7cf78e57b0794aac8b3b0de7021b5c2b
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id	oai:doaj.org-article:7cf78e57b0794aac8b3b0de7021b5c2b
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spelling	oai:doaj.org-article:7cf78e57b0794aac8b3b0de7021b5c2b2021-12-02T16:49:27ZA substrate binding model for the KEOPS tRNA modifying complex10.1038/s41467-020-19990-52041-1723https://doaj.org/article/7cf78e57b0794aac8b3b0de7021b5c2b2020-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19990-5https://doaj.org/toc/2041-1723KEOPS is an evolutionary conserved complex with a core of four core subunits—Pcc1, Kae1, Bud32 and Cgi121—that catalyzes the universal and essential tRNA modification N6-threonylcarbamoyl adenosine (t6A). Here the authors describe a Cgi121-tRNA crystal structure and new composite model of the KEOPS holo-enzyme-substrate complex that shed light on the t6A catalytic cycle and its regulation.Jonah BeenstockSamara Mishelle OnaJennifer PoratStephen OrlickyLeo C. K. WanDerek F. CeccarelliPierre MaisonneuveRachel K. SzilardZhe YinDheva SetiaputraDaniel Y. L. MaoMorgan KhanShaunak RavalDavid C. SchriemerMark A. BayfieldDaniel DurocherFrank SicheriNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-17 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jonah Beenstock Samara Mishelle Ona Jennifer Porat Stephen Orlicky Leo C. K. Wan Derek F. Ceccarelli Pierre Maisonneuve Rachel K. Szilard Zhe Yin Dheva Setiaputra Daniel Y. L. Mao Morgan Khan Shaunak Raval David C. Schriemer Mark A. Bayfield Daniel Durocher Frank Sicheri A substrate binding model for the KEOPS tRNA modifying complex
description	KEOPS is an evolutionary conserved complex with a core of four core subunits—Pcc1, Kae1, Bud32 and Cgi121—that catalyzes the universal and essential tRNA modification N6-threonylcarbamoyl adenosine (t6A). Here the authors describe a Cgi121-tRNA crystal structure and new composite model of the KEOPS holo-enzyme-substrate complex that shed light on the t6A catalytic cycle and its regulation.
format	article
author	Jonah Beenstock Samara Mishelle Ona Jennifer Porat Stephen Orlicky Leo C. K. Wan Derek F. Ceccarelli Pierre Maisonneuve Rachel K. Szilard Zhe Yin Dheva Setiaputra Daniel Y. L. Mao Morgan Khan Shaunak Raval David C. Schriemer Mark A. Bayfield Daniel Durocher Frank Sicheri
author_facet	Jonah Beenstock Samara Mishelle Ona Jennifer Porat Stephen Orlicky Leo C. K. Wan Derek F. Ceccarelli Pierre Maisonneuve Rachel K. Szilard Zhe Yin Dheva Setiaputra Daniel Y. L. Mao Morgan Khan Shaunak Raval David C. Schriemer Mark A. Bayfield Daniel Durocher Frank Sicheri
author_sort	Jonah Beenstock
title	A substrate binding model for the KEOPS tRNA modifying complex
title_short	A substrate binding model for the KEOPS tRNA modifying complex
title_full	A substrate binding model for the KEOPS tRNA modifying complex
title_fullStr	A substrate binding model for the KEOPS tRNA modifying complex
title_full_unstemmed	A substrate binding model for the KEOPS tRNA modifying complex
title_sort	substrate binding model for the keops trna modifying complex
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/7cf78e57b0794aac8b3b0de7021b5c2b
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A substrate binding model for the KEOPS tRNA modifying complex

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