학술논문
Nucleotide binding by the widespread high-affinity cyclic di-GMP receptor MshEN domain
Document Type
article
Author
Source
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
Subject
Language
English
ISSN
2041-1723
Abstract
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.