9VLH
Crystal structure of Bacillus subtilis DegQ tetramer
Summary for 9VLH
Entry DOI | 10.2210/pdb9vlh/pdb |
Related | 9VLI |
Descriptor | Degradation enzyme regulation protein DegQ (2 entities in total) |
Functional Keywords | transcription regulatory protein, transcription |
Biological source | Bacillus subtilis |
Total number of polymer chains | 8 |
Total formula weight | 44443.55 |
Authors | Fujimoto, Z.,Kishine, N.,Kimura, K. (deposition date: 2025-06-25, release date: 2025-09-24, Last modification date: 2025-10-08) |
Primary citation | Fujimoto, Z.,Kishine, N.,Saitou, K.,Kimura, K. Tetrameric structure of Bacillus subtilis DegQ and its predicted interaction with the DegS-DegU two-component system. Acta Crystallogr.,Sect.F, 81:425-433, 2025 Cited by PubMed Abstract: Bacillus subtilis DegQ is a 46-amino-acid regulatory protein involved in the DegS-DegU two-component system. DegQ promotes the phosphorylation of DegU by DegS, switching the function of DegU from competence to the induction of poly-γ-glutamate production. To elucidate its structural role, we determined the crystal structures of wild-type DegQ and its mutant DegQS25L. Each DegQ monomer folds into a single α-helix, and four monomers assemble into a tetramer characterized by a four-helix coiled-coil structure. Within the tetramer, two adjacent helices are oriented in the same direction, while the other two are oriented oppositely, forming a pseudo-twofold symmetric arrangement. The mutant form displays disrupted symmetry due to altered helix packing, which is caused by shifts in the coiled-coil heptad register induced by the mutation. Structural predictions using AlphaFold3 suggest that DegQ likely binds to the N-terminal helix bundle of DegS, either as a dimer or as individual monomers. These findings provide structural insight into DegQ oligomerization and its potential role in modulating DegS autophosphorylation and DegU binding. PubMed: 40937771DOI: 10.1107/S2053230X25007903 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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