7CD2
Crystal structure of the S103F mutant of Bacillus subtilis (natto) YabJ protein.
Summary for 7CD2
| Entry DOI | 10.2210/pdb7cd2/pdb |
| Related | 5Y6U |
| Descriptor | YabJ protein (1 entity in total) |
| Functional Keywords | mutant, homotetramer, unknown function |
| Biological source | Bacillus subtilis subsp. natto (strain BEST195) |
| Total number of polymer chains | 20 |
| Total formula weight | 274553.28 |
| Authors | Fujimoto, Z.,Kishine, N.,Kimura, K. (deposition date: 2020-06-18, release date: 2021-03-03, Last modification date: 2024-11-20) |
| Primary citation | Fujimoto, Z.,Hong, L.T.T.,Kishine, N.,Suzuki, N.,Kimura, K. Tetramer formation of Bacillus subtilis YabJ protein that belongs to YjgF/YER057c/UK114 family. Biosci.Biotechnol.Biochem., 85:297-306, 2021 Cited by PubMed Abstract: Bacillus subtilis YabJ protein belongs to the highly conserved YjgF/YER057c/UK114 family, which has a homotrimeric quaternary structure. The dominant allele of yabJ gene that is caused by a single amino acid mutation of Ser103Phe enables poly-γ-glutamic acid (γPGA) production of B. subtilis under conditions where the cell-density signal transduction was disturbed by the loss of DegQ function. X-ray crystallography of recombinant proteins revealed that unlike the homotrimeric wild-type YabJ, the mutant YabJ(Ser103Phe) had a homotetrameric quaternary structure, and the structural change appeared to be triggered by an inversion of the fifth β-strand. The YabJ homotetramer has a hole that is highly accessible, penetrating through the tetramer, and 2 surface concaves as potential ligand-binding sites. Western blot analyses revealed that the conformational change was also induced in vivo by the Ser103Phe mutation. PubMed: 33590041DOI: 10.1093/bbb/zbaa037 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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