3ZTB
The bacterial stressosome: a modular system that has been adapted to control secondary messenger signaling
3ZTB の概要
| エントリーDOI | 10.2210/pdb3ztb/pdb |
| 関連するPDBエントリー | 2VY9 3ZT9 3ZTA 3ZXN |
| 分子名称 | ANTI-SIGMA-FACTOR ANTAGONIST (STAS) DOMAIN PROTEIN, IODIDE ION (3 entities in total) |
| 機能のキーワード | signaling, stressosome, signal transduction, phosphorylation, protein-protein interaction, type 2c phosphatases, rsbs |
| 由来する生物種 | MOORELLA THERMOACETICA |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 27575.69 |
| 構造登録者 | Quin, M.B.,Berrisford, J.M.,Newman, J.A.,Basle, A.,Lewis, R.J.,Marles-Wright, J. (登録日: 2011-07-06, 公開日: 2012-02-22, 最終更新日: 2024-10-16) |
| 主引用文献 | Quin, M.B.,Berrisford, J.M.,Newman, J.A.,Basle, A.,Lewis, R.J.,Marles-Wright, J. The Bacterial Stressosome: A Modular System that Has Been Adapted to Control Secondary Messenger Signaling. Structure, 20:350-, 2012 Cited by PubMed Abstract: The stressosome complex regulates downstream effectors in response to environmental signals. In Bacillus subtilis, it activates the alternative sigma factor σ(B), leading to the upregulation of the general stress regulon. Herein, we characterize a stressosome-regulated biochemical pathway in Moorella thermoacetica. We show that the presumed sensor, MtR, and the scaffold, MtS, form a pseudo-icosahedral structure like that observed in B. subtilis. The N-terminal domain of MtR is structurally homologous to B. subtilis RsbR, despite low sequence identity. The affinity of the switch kinase, MtT, for MtS decreases following MtS phosphorylation and not because of structural reorganization. Dephosphorylation of MtS by the PP2C type phosphatase MtX permits the switch kinase to rebind the stressosome to reset the response. We also show that MtT regulates cyclic di-GMP biosynthesis through inhibition of a GG(D/E)EF-type diguanylate cyclase, demonstrating that secondary messenger levels are regulated by the stressosome. PubMed: 22325782DOI: 10.1016/J.STR.2012.01.003 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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