7CD2

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

7CD2 の概要

• エントリーDOI: 10.2210/pdb7cd2/pdb
• 関連するPDBエントリー: 5Y6U
• 分子名称: YabJ protein (1 entity in total)
• 機能のキーワード: mutant, homotetramer, unknown function
• 由来する生物種: Bacillus subtilis subsp. natto (strain BEST195)
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 274553.28

構造登録者

Fujimoto, Z.,Kishine, N.,Kimura, K. (登録日: 2020-06-18, 公開日: 2021-03-03, 最終更新日: 2024-11-20)

主引用文献

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

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: 33590041
DOI: 10.1093/bbb/zbaa037

実験手法

X-RAY DIFFRACTION (2.7 Å)