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TitleStructures of the FleQ-FleN master regulators reveal large-scale conformational switching in motility and biofilm control.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 120, Issue 50, Page e2312276120, Year 2023
Publish dateDec 12, 2023
AuthorsLucía Torres-Sánchez / Thibault Géry Sana / Marion Decossas / Yaser Hashem / Petya Violinova Krasteva /
PubMed Abstract can cause a wide array of chronic and acute infections associated with its ability to rapidly switch between planktonic, biofilm, and dispersed lifestyles, each with a specific arsenal for bacterial ... can cause a wide array of chronic and acute infections associated with its ability to rapidly switch between planktonic, biofilm, and dispersed lifestyles, each with a specific arsenal for bacterial survival and virulence. At the cellular level, many of the physiological transitions are orchestrated by the intracellular second messenger c-di-GMP and its receptor-effector FleQ. A bacterial enhancer binding protein, FleQ acts as a master regulator of both flagellar motility and adherence factor secretion and uses remarkably different transcription activation mechanisms depending on its dinucleotide loading state, adenosine triphosphatase (ATPase) activity, interactions with polymerase sigma (σ) factors, and complexation with a second ATPase, FleN. How the FleQ-FleN tandem can exert diverse effects through recognition of a conserved FleQ binding consensus has remained enigmatic. Here, we provide cryogenic electron microscopy (cryo-EM) structures of both c-di-GMP-bound and c-di-GMP-free FleQ-FleN complexes which deepen our understanding of the proteins' (di)nucleotide-dependent conformational switching and fine-tuned roles in gene expression regulation.
External linksProc Natl Acad Sci U S A / PubMed:38051770 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.3 Å
Structure data

17445

8p53

EMDB-17445, PDB-8p53:
Cryo-EM structure of the c-di-GMP-free FleQ-FleN master regulator complex of P. aeruginosa
Method: EM (single particle) / Resolution: 2.7 Å

17581

8pb9

EMDB-17581, PDB-8pb9:
Cryo-EM structure of the c-di-GMP-bound FleQ-FleN master regulator complex from Pseudomonas aeruginosa
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ACP:
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / AMP-PCP, energy-carrying molecule analogue*YM

ChemComp-C2E:
9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one) / Cyclic di-GMP

Source
  • pseudomonas aeruginosa pao1 (bacteria)
KeywordsGENE REGULATION / Pseudomonas aeruginosa / biofilm / c-di-GMP / transcription regulation / Biofilm formation / c-di-GMP signaling / second messengers / bacterial secretion / bEBPs

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