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8P53

Cryo-EM structure of the c-di-GMP-free FleQ-FleN master regulator complex of P. aeruginosa

Summary for 8P53
Entry DOI10.2210/pdb8p53/pdb
EMDB information17445
DescriptorAntiactivator FleN, Transcriptional regulator FleQ, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordspseudomonas aeruginosa, biofilm, c-di-gmp, transcription regulation, gene regulation
Biological sourcePseudomonas aeruginosa PAO1
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Total number of polymer chains6
Total formula weight289508.19
Authors
Torres-Sanchez, L.,Krasteva, P.V. (deposition date: 2023-05-23, release date: 2023-12-13)
Primary citationTorres-Sanchez, L.,Gery Sana, T.,Decossas, M.,Hashem, Y.,Krasteva, P.V.
Structures of the P. aeruginosa FleQ-FleN master regulators reveal large-scale conformational switching in motility and biofilm control.
Proc.Natl.Acad.Sci.USA, 120:e2312276120-e2312276120, 2023
Cited by
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 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.
PubMed: 38051770
DOI: 10.1073/pnas.2312276120
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.7 Å)
Structure validation

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