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.
Guardado en:
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 |
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Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2016
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Materias: | |
Acceso en línea: | https://doaj.org/article/69073df07bab47839c41ed1768992ae2 |
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