7X7H
Crystal structure of Fructose regulator/Histidine phosphocarrier protein complex from Vibrio cholerae
Summary for 7X7H
| Entry DOI | 10.2210/pdb7x7h/pdb |
| Descriptor | Catabolite repressor/activator, HPr family phosphocarrier protein, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | pts, vibrio, fructose, transcriptional regulator, galr/laci, hpr, gene regulation, gene regulation-transferase complex, gene regulation/transferase |
| Biological source | Vibrio cholerae More |
| Total number of polymer chains | 4 |
| Total formula weight | 92048.62 |
| Authors | Kim, M.-K.,Zhang, J.,Yoon, C.-K.,Seok, Y.-J. (deposition date: 2022-03-09, release date: 2023-03-15, Last modification date: 2024-05-29) |
| Primary citation | Yoon, C.K.,Lee, S.H.,Zhang, J.,Lee, H.Y.,Kim, M.K.,Seok, Y.J. HPr prevents FruR-mediated facilitation of RNA polymerase binding to the fru promoter in Vibrio cholerae. Nucleic Acids Res., 51:5432-5448, 2023 Cited by PubMed Abstract: Phosphorylation state-dependent interactions of the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS) components with transcription factors play a key role in carbon catabolite repression (CCR) by glucose in bacteria. Glucose inhibits the PTS-dependent transport of fructose and is preferred over fructose in Vibrio cholerae, but the mechanism is unknown. We have recently shown that, contrary to Escherichia coli, the fructose-dependent transcriptional regulator FruR acts as an activator of the fru operon in V. cholerae and binding of the FruR-fructose 1-phosphate (F1P) complex to an operator facilitates RNA polymerase (RNAP) binding to the fru promoter. Here we show that, in the presence of glucose, dephosphorylated HPr, a general PTS component, binds to FruR. Whereas HPr does not affect DNA-binding affinity of FruR, regardless of the presence of F1P, it prevents the FruR-F1P complex from facilitating the binding of RNAP to the fru promoter. Structural and biochemical analyses of the FruR-HPr complex identify key residues responsible for the V. cholerae-specific FruR-HPr interaction not observed in E. coli. Finally, we reveal how the dephosphorylated HPr interacts with FruR in V. cholerae, whereas the phosphorylated HPr binds to CcpA, which is a global regulator of CCR in Bacillus subtilis and shows structural similarity to FruR. PubMed: 36987873DOI: 10.1093/nar/gkad220 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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