4R22
TnrA-DNA complex
4R22 の概要
| エントリーDOI | 10.2210/pdb4r22/pdb |
| 関連するPDBエントリー | 4R24 4R25 |
| 分子名称 | HTH-type transcriptional regulator TnrA, DNA (5'-D(*CP*GP*TP*GP*TP*AP*AP*GP*GP*AP*AP*TP*TP*CP*TP*GP*AP*CP*AP*CP*G)-3') (2 entities in total) |
| 機能のキーワード | new family of transcription regulators, transcription, gs, transcription-dna complex, transcription/dna |
| 由来する生物種 | Bacillus megaterium 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 16195.33 |
| 構造登録者 | |
| 主引用文献 | Schumacher, M.A.,Chinnam, N.B.,Cuthbert, B.,Tonthat, N.K.,Whitfill, T. Structures of regulatory machinery reveal novel molecular mechanisms controlling B. subtilis nitrogen homeostasis. Genes Dev., 29:451-464, 2015 Cited by PubMed Abstract: All cells must sense and adapt to changing nutrient availability. However, detailed molecular mechanisms coordinating such regulatory pathways remain poorly understood. In Bacillus subtilis, nitrogen homeostasis is controlled by a unique circuitry composed of the regulator TnrA, which is deactivated by feedback-inhibited glutamine synthetase (GS) during nitrogen excess and stabilized by GlnK upon nitrogen depletion, and the repressor GlnR. Here we describe a complete molecular dissection of this network. TnrA and GlnR, the global nitrogen homeostatic transcription regulators, are revealed as founders of a new structural family of dimeric DNA-binding proteins with C-terminal, flexible, effector-binding sensors that modulate their dimerization. Remarkably, the TnrA sensor domains insert into GS intersubunit catalytic pores, destabilizing the TnrA dimer and causing an unprecedented GS dodecamer-to-tetradecamer conversion, which concomitantly deactivates GS. In contrast, each subunit of the GlnK trimer "templates" active TnrA dimers. Unlike TnrA, GlnR sensors mediate an autoinhibitory dimer-destabilizing interaction alleviated by GS, which acts as a GlnR chaperone. Thus, these studies unveil heretofore unseen mechanisms by which inducible sensor domains drive metabolic reprograming in the model Gram-positive bacterium B. subtilis. PubMed: 25691471DOI: 10.1101/gad.254714.114 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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