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.
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Publishing Group
2016-08-01
|
| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms12481 |