4RX6
Structure of B. subtilis GlnK-ATP complex to 2.6 Angstrom
4RX6 の概要
エントリーDOI | 10.2210/pdb4rx6/pdb |
関連するPDBエントリー | 4R25 |
分子名称 | Nitrogen regulatory PII-like protein, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total) |
機能のキーワード | pii protein, transcription |
由来する生物種 | Bacillus subtilis subsp. subtilis |
細胞内の位置 | Cell membrane ; Peripheral membrane protein : Q07428 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 41725.79 |
構造登録者 | Schumacher, M.A.,Cuthbert, B.,Tonthat, N.,Chinnam, N.G.,Whitfill, T. (登録日: 2014-12-09, 公開日: 2015-12-30, 最終更新日: 2023-09-20) |
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 (2.5994 Å) |
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