Differential ligand-selective control of opposing enzymatic activities within a bifunctional c-di-GMP enzyme
Dayna C. Patterson, Myrrh Perez Ruiz, Hyerin Yoon, Johnnie A. Walker, Jean‐Paul Armache, Neela H. Yennawar, Emily E. Weinert
Abstract
in response to gaseous environment, with nitric oxide conditions leading to the greatest amount of biofilm formation. The ability of DcpG to differentially control GGDEF and EAL domain activity in response to ligand binding is likely due to the unusual properties of the globin domain, including rapid ligand dissociation rates and high midpoint potentials. Using structural information from small-angle X-ray scattering and negative stain electron microscopy studies, we developed a structural model of DcpG, providing information about the regulatory mechanism. These studies provide information about full-length GCS protein architecture and insight into the mechanism by which a single regulatory domain can selectively control output domains with opposing enzymatic activities.