Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity

Cytidine deaminases are evolutionarily conserved enzymes that edit genomes by deaminating cytidine to uridine. Here the authors present the crystal structure of APOBEC3A with a single-stranded DNA substrate bound in the active site to shed light on the mechanism and specificity of substrate recognit...

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Autores principales:	Takahide Kouno, Tania V. Silvas, Brendan J. Hilbert, Shivender M. D. Shandilya, Markus F. Bohn, Brian A. Kelch, William E. Royer, Mohan Somasundaran, Nese Kurt Yilmaz, Hiroshi Matsuo, Celia A. Schiffer
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/d9aff862807c4ea9832b5ce81ea7e7e9
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spelling	oai:doaj.org-article:d9aff862807c4ea9832b5ce81ea7e7e92021-12-02T14:42:21ZCrystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity10.1038/ncomms150242041-1723https://doaj.org/article/d9aff862807c4ea9832b5ce81ea7e7e92017-04-01T00:00:00Zhttps://doi.org/10.1038/ncomms15024https://doaj.org/toc/2041-1723Cytidine deaminases are evolutionarily conserved enzymes that edit genomes by deaminating cytidine to uridine. Here the authors present the crystal structure of APOBEC3A with a single-stranded DNA substrate bound in the active site to shed light on the mechanism and specificity of substrate recognition.Takahide KounoTania V. SilvasBrendan J. HilbertShivender M. D. ShandilyaMarkus F. BohnBrian A. KelchWilliam E. RoyerMohan SomasundaranNese Kurt YilmazHiroshi MatsuoCelia A. SchifferNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-8 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Takahide Kouno Tania V. Silvas Brendan J. Hilbert Shivender M. D. Shandilya Markus F. Bohn Brian A. Kelch William E. Royer Mohan Somasundaran Nese Kurt Yilmaz Hiroshi Matsuo Celia A. Schiffer Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity
description	Cytidine deaminases are evolutionarily conserved enzymes that edit genomes by deaminating cytidine to uridine. Here the authors present the crystal structure of APOBEC3A with a single-stranded DNA substrate bound in the active site to shed light on the mechanism and specificity of substrate recognition.
format	article
author	Takahide Kouno Tania V. Silvas Brendan J. Hilbert Shivender M. D. Shandilya Markus F. Bohn Brian A. Kelch William E. Royer Mohan Somasundaran Nese Kurt Yilmaz Hiroshi Matsuo Celia A. Schiffer
author_facet	Takahide Kouno Tania V. Silvas Brendan J. Hilbert Shivender M. D. Shandilya Markus F. Bohn Brian A. Kelch William E. Royer Mohan Somasundaran Nese Kurt Yilmaz Hiroshi Matsuo Celia A. Schiffer
author_sort	Takahide Kouno
title	Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity
title_short	Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity
title_full	Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity
title_fullStr	Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity
title_full_unstemmed	Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity
title_sort	crystal structure of apobec3a bound to single-stranded dna reveals structural basis for cytidine deamination and specificity
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/d9aff862807c4ea9832b5ce81ea7e7e9
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Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity

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