8HML

Co-crystal structure of the C terminal DNA binding domain of Saccharopolyspora erythraea GlnR in complex with its conserved promoter DNA in 2.95 Angstrom resolution

8HML の概要

• エントリーDOI: 10.2210/pdb8hml/pdb
• 分子名称: DNA-binding response OmpR family regulator, DNA (5'-D(*AP*CP*GP*TP*AP*AP*CP*AP*TP*CP*GP*CP*GP*GP*TP*AP*AP*CP*AP*C)-3'), DNA (5'-D(*GP*TP*GP*TP*TP*AP*CP*CP*GP*CP*GP*AP*TP*GP*TP*TP*AP*CP*GP*T)-3'), ... (4 entities in total)
• 機能のキーワード: methylenetetrahydrofolate reductase, transferase-dna complex, transferase/dna
• 由来する生物種: Saccharopolyspora erythraea NRRL 2338; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 44616.65

構造登録者

Lin, W.,Xu, J.C. (登録日: 2022-12-04, 公開日: 2023-06-07, 最終更新日: 2024-05-29)

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

X-RAY DIFFRACTION (2.95 Å)