7cd4

Crystal structure of the S103F mutant of Bacillus subtilis (natto) YabJ protein.

spinqualitylabelsall models 7cd4, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: BTB, CL, MG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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-gamma-glutamic acid (gammaPGA) 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 beta-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. Tetramer formation of Bacillus subtilis YabJ protein that belongs to YjgF/YER057c/UK114 family.,Fujimoto Z, Hong LTT, Kishine N, Suzuki N, Kimura K Biosci Biotechnol Biochem. 2021 Feb 18;85(2):297-306. doi: 10.1093/bbb/zbaa037. PMID:33590041 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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