6P1C
Transcription antitermination factor Q21, SeMet-derivative
6P1C の概要
エントリーDOI | 10.2210/pdb6p1c/pdb |
分子名称 | Q protein, CHLORIDE ION (3 entities in total) |
機能のキーワード | rna polymerase, dna binding, transcription, q-dependent antitermination, q antitermination factor, gene regulation |
由来する生物種 | Phage 21 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 19079.41 |
構造登録者 | |
主引用文献 | Yin, Z.,Kaelber, J.T.,Ebright, R.H. Structural basis of Q-dependent antitermination. Proc.Natl.Acad.Sci.USA, 116:18384-18390, 2019 Cited by PubMed Abstract: Lambdoid bacteriophage Q protein mediates the switch from middle to late bacteriophage gene expression by enabling RNA polymerase (RNAP) to read through transcription terminators preceding bacteriophage late genes. Q loads onto RNAP engaged in promoter-proximal pausing at a Q binding element (QBE) and adjacent sigma-dependent pause element (SDPE) to yield a Q-loading complex, and Q subsequently translocates with RNAP as a pausing-deficient, termination-deficient Q-loaded complex. Here, we report high-resolution structures of 4 states on the pathway of antitermination by Q from bacteriophage 21 (Q21): Q21, the Q21-QBE complex, the Q21-loading complex, and the Q21-loaded complex. The results show that Q21 forms a torus, a "nozzle," that narrows and extends the RNAP RNA-exit channel, extruding topologically linked single-stranded RNA and preventing the formation of pause and terminator hairpins. PubMed: 31455742DOI: 10.1073/pnas.1909801116 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.005 Å) |
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