4LJZ
Crystal Structure Analysis of the E.coli holoenzyme
4LJZ の概要
エントリーDOI | 10.2210/pdb4ljz/pdb |
分子名称 | DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (7 entities in total) |
機能のキーワード | dna directed rna polymerase, transferase |
由来する生物種 | Escherichia coli 詳細 |
細胞内の位置 | Cytoplasm (Potential): P00579 |
タンパク質・核酸の鎖数 | 12 |
化学式量合計 | 859651.66 |
構造登録者 | |
主引用文献 | Bae, B.,Davis, E.,Brown, D.,Campbell, E.A.,Wigneshweraraj, S.,Darst, S.A. Phage T7 Gp2 inhibition of Escherichia coli RNA polymerase involves misappropriation of sigma 70 domain 1.1. Proc.Natl.Acad.Sci.USA, 110:19772-19777, 2013 Cited by PubMed Abstract: Bacteriophage T7 encodes an essential inhibitor of the Escherichia coli host RNA polymerase (RNAP), the product of gene 2 (Gp2). We determined a series of X-ray crystal structures of E. coli RNAP holoenzyme with or without Gp2. The results define the structure and location of the RNAP σ(70) subunit domain 1.1(σ(1.1)(70)) inside the RNAP active site channel, where it must be displaced by the DNA upon formation of the open promoter complex. The structures and associated data, combined with previous results, allow for a complete delineation of the mechanism for Gp2 inhibition of E. coli RNAP. In the primary inhibition mechanism, Gp2 forms a protein-protein interaction with σ(1.1)(70), preventing the normal egress of σ(1.1)(70) from the RNAP active site channel. Gp2 thus misappropriates a domain of the RNAP holoenzyme, σ(1.1)(70), to inhibit the function of the enzyme. PubMed: 24218560DOI: 10.1073/pnas.1314576110 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.5871 Å) |
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