2WNM
Solution structure of Gp2
2WNM の概要
| エントリーDOI | 10.2210/pdb2wnm/pdb |
| 分子名称 | GENE 2 (1 entity in total) |
| 機能のキーワード | small protein inhibntor bacterial rna polymerase, hydrolase |
| 由来する生物種 | ENTEROBACTERIA PHAGE T7 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 7180.98 |
| 構造登録者 | Camara, B.,Liu, M.,Shadrinc, A.,Liu, B.,Simpson, P.,Weinzierl, R.,Severinovc, K.,Cota, E.,Matthews, S.,Wigneshweraraj, S.R. (登録日: 2009-07-13, 公開日: 2010-02-16, 最終更新日: 2024-05-15) |
| 主引用文献 | Camara, B.,Liu, M.,Reynolds, J.,Shadrin, A.,Liu, B.,Kwok, K.,Simpson, P.,Weinzierl, R.,Severinov, K.,Cota, E.,Matthews, S.,Wigneshweraraj, S.R. T7 Phage Protein Gp2 Inhibits the Escherichia Coli RNA Polymerase by Antagonizing Stable DNA Strand Separation Near the Transcription Start Site. Proc.Natl.Acad.Sci.USA, 107:2247-, 2010 Cited by PubMed Abstract: Infection of Escherichia coli by the T7 phage leads to rapid and selective inhibition of the host RNA polymerase (RNAP)--a multi-subunit enzyme responsible for gene transcription--by a small ( approximately 7 kDa) phage-encoded protein called Gp2. Gp2 is also a potent inhibitor of E. coli RNAP in vitro. Here we describe the first atomic resolution structure of Gp2, which reveals a distinct run of surface-exposed negatively charged amino acid residues on one side of the molecule. Our comprehensive mutagenesis data reveal that two conserved arginine residues located on the opposite side of Gp2 are important for binding to and inhibition of RNAP. Based on a structural model of the Gp2-RNAP complex, we propose that inhibition of transcription by Gp2 involves prevention of RNAP-promoter DNA interactions required for stable DNA strand separation and maintenance of the "transcription bubble" near the transcription start site, an obligatory step in the formation of a transcriptionally competent promoter complex. PubMed: 20133868DOI: 10.1073/PNAS.0907908107 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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