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8p53

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

Structural highlights

8p53 is a 6 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.7Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FLEN_PSEAE ATPase that plays an important role in maintaining flagellar number in Pseudomonas aeruginosa (PubMed:10629180, PubMed:28065505). Exhibits anti-activator activity against FleQ, the global transcriptional regulator of flagellar genes (PubMed:22581773, PubMed:28065505).^[1] ^[2] ^[3]

Publication Abstract from PubMed

Pseudomonas aeruginosa 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 (sigma) 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.

Structures of the P. aeruginosa FleQ-FleN master regulators reveal large-scale conformational switching in motility and biofilm control.,Torres-Sanchez L, Sana TG, Decossas M, Hashem Y, Krasteva PV Proc Natl Acad Sci U S A. 2023 Dec 12;120(50):e2312276120. doi: , 10.1073/pnas.2312276120. Epub 2023 Dec 5. PMID:38051770^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Dasgupta N, Arora SK, Ramphal R. fleN, a gene that regulates flagellar number in Pseudomonas aeruginosa. J Bacteriol. 2000 Jan;182(2):357-64. PMID:10629180 doi:10.1128/JB.182.2.357-364.2000
↑ Baraquet C, Murakami K, Parsek MR, Harwood CS. The FleQ protein from Pseudomonas aeruginosa functions as both a repressor and an activator to control gene expression from the pel operon promoter in response to c-di-GMP. Nucleic Acids Res. 2012 Aug;40(15):7207-18. PMID:22581773 doi:10.1093/nar/gks384
↑ Chanchal, Banerjee P, Jain D. ATP-Induced Structural Remodeling in the Antiactivator FleN Enables Formation of the Functional Dimeric Form. Structure. 2017 Feb 7;25(2):243-252. doi: 10.1016/j.str.2016.11.022. Epub 2017, Jan 5. PMID:28065505 doi:http://dx.doi.org/10.1016/j.str.2016.11.022
↑ Torres-Sánchez L, Sana TG, Decossas M, Hashem Y, Krasteva PV. Structures of the P. aeruginosa FleQ-FleN master regulators reveal large-scale conformational switching in motility and biofilm control. Proc Natl Acad Sci U S A. 2023 Dec 12;120(50):e2312276120. PMID:38051770 doi:10.1073/pnas.2312276120