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6G8G

Flavonoid-responsive Regulator FrrA in complex with Genistein

Summary for 6G8G
Entry DOI10.2210/pdb6g8g/pdb
DescriptorTetR/AcrR family transcriptional regulator, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID, GENISTEIN (3 entities in total)
Functional Keywordsflavonoids, repressor, tetr-family, transcription
Biological sourceBradyrhizobium diazoefficiens
Total number of polymer chains4
Total formula weight97955.52
Authors
Werner, N.,Hoppen, J.,Palm, G.,Werten, S.,Goettfert, M.,Hinrichs, W. (deposition date: 2018-04-08, release date: 2019-04-17, Last modification date: 2024-10-16)
Primary citationWerner, N.,Werten, S.,Hoppen, J.,Palm, G.J.,Gottfert, M.,Hinrichs, W.
The induction mechanism of the flavonoid-responsive regulator FrrA.
Febs J., 2021
Cited by
PubMed Abstract: Bradyrhizobium diazoefficiens, a bacterial symbiont of soybean and other leguminous plants, enters a nodulation-promoting genetic programme in the presence of host-produced flavonoids and related signalling compounds. Here, we describe the crystal structure of an isoflavonoid-responsive regulator (FrrA) from Bradyrhizobium, as well as cocrystal structures with inducing and noninducing ligands (genistein and naringenin, respectively). The structures reveal a TetR-like fold whose DNA-binding domain is capable of adopting a range of orientations. A single molecule of either genistein or naringenin is asymmetrically bound in a central cavity of the FrrA homodimer, mainly via C-H contacts to the π-system of the ligands. Strikingly, however, the interaction does not provoke any conformational changes in the repressor. Both the flexible positioning of the DNA-binding domain and the absence of structural change upon ligand binding are corroborated by small-angle X-ray scattering (SAXS) experiments in solution. Together with a model of the promoter-bound state of FrrA our results suggest that inducers act as a wedge, preventing the DNA-binding domains from moving close enough together to interact with successive positions of the major groove of the palindromic operator.
PubMed: 34314575
DOI: 10.1111/febs.16141
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

231029

數據於2025-02-05公開中

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