7E6G

Crystal structure of diguanylate cyclase SiaD in complex with its activator SiaC from Pseudomonas aeruginosa

Summary for 7E6G

• Entry DOI: 10.2210/pdb7e6g/pdb
• Descriptor: Putative GGDEF domain protein, DUF1987 domain-containing protein, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: diguanylate cyclase, activation, pseudomonas aeruginosa, biosynthetic protein, de novo protein
• Biological source: Pseudomonas aeruginosa; More
• Total number of polymer chains: 6
• Total formula weight: 122342.30

Authors

Zhou, J.S.,Zhang, L.,Zhang, L. (deposition date: 2021-02-22, release date: 2021-09-22, Last modification date: 2023-11-29)

Primary citation

Chen, G.,Zhou, J.,Zuo, Y.,Huo, W.,Peng, J.,Li, M.,Zhang, Y.,Wang, T.,Zhang, L.,Zhang, L.,Liang, H.
Structural basis for diguanylate cyclase activation by its binding partner in Pseudomonas aeruginosa .
Elife, 10:-, 2021

PubMed Abstract: Cyclic-di-guanosine monophosphate (c-di-GMP) is an important effector associated with acute-chronic infection transition in . Previously, we reported a signaling network SiaABCD, which regulates biofilm formation by modulating c-di-GMP level. However, the mechanism for SiaD activation by SiaC remains elusive. Here we determine the crystal structure of SiaC-SiaD-GpCpp complex and revealed a unique mirror symmetric conformation: two SiaD form a dimer with long stalk domains, while four SiaC bind to the conserved motifs on the stalks of SiaD and stabilize the conformation for further enzymatic catalysis. Furthermore, SiaD alone exhibits an inactive pentamer conformation in solution, demonstrating that SiaC activates SiaD through a dynamic mechanism of promoting the formation of active SiaD dimers. Mutagenesis assay confirmed that the stalks of SiaD are necessary for its activation. Together, we reveal a novel mechanism for DGC activation, which clarifies the regulatory networks of c-di-GMP signaling.

PubMed: 34498587
DOI: 10.7554/eLife.67289

Experimental method

X-RAY DIFFRACTION (2.65 Å)