Abstract
Cyclic diguanosine monophosphate nucleotide (cyclic di-GMP) has emerged as a crucial second messenger molecule that responds to a wide variety of environmental cues in almost all bacteria. Several canonical binding modes of cyclic di-GMP interactions with its protein or riboswitch targets have been described. However, more cyclic di-GMP binding proteins are expected to exist, due to the wide variety of biological activities that can be controlled by this flexible molecule. In this chapter, we review some of the lesser known but equally interesting cyclic di-GMP binding modes that have been discovered by our group in the past few years, including (1) cyclic di-GMP binding in the active site of a diguanylate cyclase containing the canonical GGDEF motif without an inhibitory site; (2) a PilZ domain structure that is interrupted in the middle by two long helices and self-assembles into a tetramer via the leucine-rich heptad repeat; and (3) a new bulge conformation of cyclic di-GMP with one guanine base flipping from anti to syn in binding to a degenerate EAL domain.
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Acknowledgments
This work was supported by the Ministry of Education, Taiwan, ROC under the ATU plan, and by the National Science Council, Taiwan, ROC (Grants 102-2113-M005-006-MY3 to SH Chou) and by the NIH Intramural Research Program at the National Library of Medicine (MYG).
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Chou, SH., Galperin, M.Y. (2020). Noncanonical Cyclic di-GMP Binding Modes. In: Chou, SH., Guiliani, N., Lee, V., Römling, U. (eds) Microbial Cyclic Di-Nucleotide Signaling. Springer, Cham. https://doi.org/10.1007/978-3-030-33308-9_8
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DOI: https://doi.org/10.1007/978-3-030-33308-9_8
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