7TFC の概要
| エントリーDOI | 10.2210/pdb7tfc/pdb |
| EMDBエントリー | 25869 |
| 分子名称 | Glutamine synthetase, GlnR C-tail peptide, MAGNESIUM ION, ... (4 entities in total) |
| 機能のキーワード | glutamine synthetase repressor tetradecamer, biosynthetic protein, ligase |
| 由来する生物種 | Bacillus subtilis 詳細 |
| タンパク質・核酸の鎖数 | 28 |
| 化学式量合計 | 755308.39 |
| 構造登録者 | |
| 主引用文献 | Travis, B.A.,Peck, J.V.,Salinas, R.,Dopkins, B.,Lent, N.,Nguyen, V.D.,Borgnia, M.J.,Brennan, R.G.,Schumacher, M.A. Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria. Nat Commun, 13:3793-3793, 2022 Cited by PubMed Abstract: How bacteria sense and respond to nitrogen levels are central questions in microbial physiology. In Gram-positive bacteria, nitrogen homeostasis is controlled by an operon encoding glutamine synthetase (GS), a dodecameric machine that assimilates ammonium into glutamine, and the GlnR repressor. GlnR detects nitrogen excess indirectly by binding glutamine-feedback-inhibited-GS (FBI-GS), which activates its transcription-repression function. The molecular mechanisms behind this regulatory circuitry, however, are unknown. Here we describe biochemical and structural analyses of GS and FBI-GS-GlnR complexes from pathogenic and non-pathogenic Gram-positive bacteria. The structures show FBI-GS binds the GlnR C-terminal domain within its active-site cavity, juxtaposing two GlnR monomers to form a DNA-binding-competent GlnR dimer. The FBI-GS-GlnR interaction stabilizes the inactive GS conformation. Strikingly, this interaction also favors a remarkable dodecamer to tetradecamer transition in some GS, breaking the paradigm that all bacterial GS are dodecamers. These data thus unveil unique structural mechanisms of transcription and enzymatic regulation. PubMed: 35778410DOI: 10.1038/s41467-022-31573-0 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (1.96 Å) |
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