Nucleotide binding by the widespread high-affinity cyclic di-GMP receptor MshEN domain

Cyclic-di-GMP is a bacterial second messenger that binds to the regulatory domain of ATPases of some bacteria. Here, the authors report the crystal structure of this interaction, identify a cyclic-di-GMP binding mode, and show that this interaction might be important for bacterial biofilm formation.

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Autores principales:	Yu-Chuan Wang, Ko-Hsin Chin, Zhi-Le Tu, Jin He, Christopher J. Jones, David Zamorano Sanchez, Fitnat H. Yildiz, Michael Y. Galperin, Shan-Ho Chou
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/69073df07bab47839c41ed1768992ae2
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spelling	oai:doaj.org-article:69073df07bab47839c41ed1768992ae22021-12-02T14:38:57ZNucleotide binding by the widespread high-affinity cyclic di-GMP receptor MshEN domain10.1038/ncomms124812041-1723https://doaj.org/article/69073df07bab47839c41ed1768992ae22016-08-01T00:00:00Zhttps://doi.org/10.1038/ncomms12481https://doaj.org/toc/2041-1723Cyclic-di-GMP is a bacterial second messenger that binds to the regulatory domain of ATPases of some bacteria. Here, the authors report the crystal structure of this interaction, identify a cyclic-di-GMP binding mode, and show that this interaction might be important for bacterial biofilm formation.Yu-Chuan WangKo-Hsin ChinZhi-Le TuJin HeChristopher J. JonesDavid Zamorano SanchezFitnat H. YildizMichael Y. GalperinShan-Ho ChouNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yu-Chuan Wang Ko-Hsin Chin Zhi-Le Tu Jin He Christopher J. Jones David Zamorano Sanchez Fitnat H. Yildiz Michael Y. Galperin Shan-Ho Chou Nucleotide binding by the widespread high-affinity cyclic di-GMP receptor MshEN domain
description	Cyclic-di-GMP is a bacterial second messenger that binds to the regulatory domain of ATPases of some bacteria. Here, the authors report the crystal structure of this interaction, identify a cyclic-di-GMP binding mode, and show that this interaction might be important for bacterial biofilm formation.
format	article
author	Yu-Chuan Wang Ko-Hsin Chin Zhi-Le Tu Jin He Christopher J. Jones David Zamorano Sanchez Fitnat H. Yildiz Michael Y. Galperin Shan-Ho Chou
author_facet	Yu-Chuan Wang Ko-Hsin Chin Zhi-Le Tu Jin He Christopher J. Jones David Zamorano Sanchez Fitnat H. Yildiz Michael Y. Galperin Shan-Ho Chou
author_sort	Yu-Chuan Wang
title	Nucleotide binding by the widespread high-affinity cyclic di-GMP receptor MshEN domain
title_short	Nucleotide binding by the widespread high-affinity cyclic di-GMP receptor MshEN domain
title_full	Nucleotide binding by the widespread high-affinity cyclic di-GMP receptor MshEN domain
title_fullStr	Nucleotide binding by the widespread high-affinity cyclic di-GMP receptor MshEN domain
title_full_unstemmed	Nucleotide binding by the widespread high-affinity cyclic di-GMP receptor MshEN domain
title_sort	nucleotide binding by the widespread high-affinity cyclic di-gmp receptor mshen domain
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/69073df07bab47839c41ed1768992ae2
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Nucleotide binding by the widespread high-affinity cyclic di-GMP receptor MshEN domain

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