8HIH

Cryo-EM structure of Mycobacterium tuberculosis transcription initiation complex with transcription factor GlnR

これはPDB形式変換不可エントリーです。

8HIH の概要

• エントリーDOI: 10.2210/pdb8hih/pdb
• EMDBエントリー: 34816
• 分子名称: DNA-directed RNA polymerase subunit alpha, MAGNESIUM ION, DNA-directed RNA polymerase subunit beta, ... (10 entities in total)
• 機能のキーワード: transcription factor, transcription-dna complex, transcription/dna
• 由来する生物種: Mycobacterium tuberculosis; 詳細
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 638075.72

構造登録者

Lin, W.,Shi, J.,Xu, J.C. (登録日: 2022-11-20, 公開日: 2023-06-07, 最終更新日: 2024-07-31)

主引用文献

Shi, J.,Feng, Z.,Xu, J.,Li, F.,Zhang, Y.,Wen, A.,Wang, F.,Song, Q.,Wang, L.,Cui, H.,Tong, S.,Chen, P.,Zhu, Y.,Zhao, G.,Wang, S.,Feng, Y.,Lin, W.
Structural insights into the transcription activation mechanism of the global regulator GlnR from actinobacteria.
Proc.Natl.Acad.Sci.USA, 120:e2300282120-e2300282120, 2023

PubMed Abstract: In actinobacteria, an OmpR/PhoB subfamily protein called GlnR acts as an orphan response regulator and globally coordinates the expression of genes responsible for nitrogen, carbon, and phosphate metabolism in actinobacteria. Although many researchers have attempted to elucidate the mechanisms of GlnR-dependent transcription activation, progress is impeded by lacking of an overall structure of GlnR-dependent transcription activation complex (GlnR-TAC). Here, we report a co-crystal structure of the C-terminal DNA-binding domain of GlnR (GlnR_DBD) in complex with its regulatory -element DNA and a cryo-EM structure of GlnR-TAC which comprises RNA polymerase, GlnR, and a promoter containing four well-characterized conserved GlnR binding sites. These structures illustrate how four GlnR protomers coordinate to engage promoter DNA in a head-to-tail manner, with four N-terminal receiver domains of GlnR (GlnR-RECs) bridging GlnR_DBDs and the RNAP core enzyme. Structural analysis also unravels that GlnR-TAC is stabilized by complex protein-protein interactions between GlnR and the conserved β flap, σR4, αCTD, and αNTD domains of RNAP, which are further confirmed by our biochemical assays. Taken together, these results reveal a global transcription activation mechanism for the master regulator GlnR and other OmpR/PhoB subfamily proteins and present a unique mode of bacterial transcription regulation.

PubMed: 37216560
DOI: 10.1073/pnas.2300282120

実験手法

ELECTRON MICROSCOPY (3.66 Å)