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Function
Cyclic dimeric (3'–5') guanosine monophosphate (c-di-GMP) is a bacterial second messenger present in several biological aspects of several environmental and pathogenic bacteria. This second messenger is capable of regulating the cell cycle, biofilm formation, dispersal, motility, and virulence. The synthesis and degradation of c-diGMP are controlled by the activities of two classes of proteins: diguanylate cyclases (DGCs), with an active GGDEF domain, and specific phosphodiesterases (PDEs), with an EAL or HD-GYP domain. SiaD has DGC activity modulated by its binding partner through direct interaction with SiaC, forming the SiaC-SiaD complex.
Structural highlights
The SiaC-SiaD complex is formed by two SiaD molecules and the binding of four SiaC. The conformation of the complex is composed of two SiaD molecules (SiaD-A and SiaD-B) that form a parallel spiral through their helix rods, and their dimeric rods are stabilized by the binding of two pairs of SiaC molecules (SiaC-C /D) and SiaC-E/F), each in a different location along the dimeric stem, which may be proximal or distal to the DGC domain of SiaD. Furthermore, a non-hydrolyzable GTP analog molecule, GpCpp, was observed to bind to the active site of SiaD-A.
Disease
Relevance
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