ReviewJournal of bacteriology2016
Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms.
Review in Journal of bacteriology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 158 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
158 citing papers in PubMed, 267 citations in OpenAlex.
- Article
- To Move or Not to Move: When and How Bacteria Suppress Flagellar Motility.Molecular microbiology · 2026Review
- The versatility of the CHASE domain in one-component systems of c-di-GMP signal transduction fromJournal of bacteriology · 2026Article
- Article
- Dual-function enzyme acts as a global c-di-GMP sink and local anti sigma factor antagonist to drive cellular differentiation.PLoS genetics · 2026Article
- Rapid evolution of Klebsiella pneumoniae biofilms in vitro delineates adaptive changes selected during infection.Nature communications · 2026Article
- A dual-threshold system relying on multiple c-di-GMP metabolic enzymes controls cell fate of a cyanobacterium.PLoS biology · 2026Article
- Cyclic di-GMP suppresses cancer metastasis by targeting proteasome 26S subunit non-ATPase 3 independently of STING.Signal transduction and targeted therapy · 2026Article
- Previously Uncharacterised Aliphatic Amino Acid Positions Modulate the Apparent Catalytic Activity of the EAL Domain of ZMO_1055 and Other Cyclic Di-GMP-Specific EAL Phosphodiesterases.Microbial biotechnology · 2026Article
- Discovery of Novel c-di-GMP-Related Genes inPathogens (Basel, Switzerland) · 2026Article
- Dynamic Executors of Bacterial Signals: Functional Versatility and Regulatory Networks of c-di-GMP Effectors.Biomolecules · 2025Review
- ComFB, a widespread family of c-di-NMP receptor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- c-di-GMP-Dependent Regulation of Motility bybioRxiv : the preprint server for biology · 2025Article
- Spatio-genetically coordinated TPR domain-containing proteins modulate c-di-GMP signaling in Vibrio vulnificus.PLoS pathogens · 2025Article
- Biofilm Dispersal inMicroorganisms · 2025Article
- A WYL domain transcription factor regulates Lactiplantibacillus plantarum intestinal colonization via perceiving c-di-GMP.Nature communications · 2025Article
- c-di-GMP inhibits rRNA methylation and impairs ribosome assembly in the presence of kanamycin.EMBO reports · 2025Article
- Insertion of a Divergent GAF-like Domain Defines a Novel Family of YcgR Homologues That Bind c-di-GMP inACS omega · 2025Article
- NagZ modulates the virulence ofVirulence · 2024Article
98 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Cyclic di-GMP (c-di-GMP) synthetases and hydrolases (GGDEF, EAL, and HD-GYP domains) can be readily identified in bacterial genome sequences by using standard bioinformatic tools. In contrast, identification of c-di-GMP receptors remains a difficult task, and the current list of experimentally characterized c-di-GMP-binding proteins is likely incomplete. Several classes of c-di-GMP-binding proteins have been structurally characterized; for some others, the binding sites have been identified; and for several potential c-di-GMP receptors, the binding sites remain to be determined. We present here a comparative structural analysis of c-di-GMP-protein complexes that aims to discern the common themes in the binding mechanisms that allow c-di-GMP receptors to bind it with (sub)micromolar affinities despite the 1,000-fold excess of GTP. The available structures show that most receptors use their Arg and Asp/Glu residues to bind c-di-GMP monomers, dimers, or tetramers with stacked guanine bases. The only exception is the EAL domains that bind c-di-GMP monomers in an extended conformation. We show that in c-di-GMP-binding signature motifs, Arg residues bind to the O-6 and N-7 atoms at the Hoogsteen edge of the guanine base, while Asp/Glu residues bind the N-1 and N-2 atoms at its Watson-Crick edge. In addition, Arg residues participate in stacking interactions with the guanine bases of c-di-GMP and the aromatic rings of Tyr and Phe residues. This may account for the presence of Arg residues in the active sites of every receptor protein that binds stacked c-di-GMP. We also discuss the implications of these structural data for the improved understanding of the c-di-GMP signaling mechanisms.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.