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データを開く
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基本情報
登録情報 | データベース: SASBDB / ID: SASDDE3 |
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![]() | Human respiratory syncytial virus (HRSV) M2–1 RNA-binding core domain
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機能・相同性 | ![]() regulation of viral transcription / viral transcription / translation elongation factor activity / virion component / transcription antitermination / host cell cytoplasm / structural constituent of virion / host cell nucleus / RNA binding / metal ion binding 類似検索 - 分子機能 |
生物種 | ![]() |
![]() | ![]() タイトル: Structure and stability of the Human respiratory syncytial virus M RNA-binding core domain reveals a compact and cooperative folding unit. 著者: Ivana G Molina / Inokentijs Josts / Yasser Almeida Hernandez / Sebastian Esperante / Mariano Salgueiro / Maria M Garcia Alai / Gonzalo de Prat-Gay / Henning Tidow / ![]() ![]() 要旨: Human syncytial respiratory virus is a nonsegmented negative-strand RNA virus with serious implications for respiratory disease in infants, and has recently been reclassified into a new family, ...Human syncytial respiratory virus is a nonsegmented negative-strand RNA virus with serious implications for respiratory disease in infants, and has recently been reclassified into a new family, Pneumoviridae. One of the main reasons for this classification is the unique presence of a transcriptional antiterminator, called M. The puzzling mechanism of action of M, which is a rarity among antiterminators in viruses and is part of the RNA polymerase complex, relies on dissecting the structure and function of this multidomain tetramer. The RNA-binding activity is located in a monomeric globular `core' domain, a high-resolution crystal structure of which is now presented. The structure reveals a compact domain which is superimposable on the full-length M tetramer, with additional electron density for the C-terminal tail that was not observed in the previous models. Moreover, its folding stability was determined through chemical denaturation, which shows that the secondary and tertiary structure unfold concomitantly, which is indicative of a two-state equilibrium. These results constitute a further step in the understanding of this unique RNA-binding domain, for which there is no sequence or structural counterpart outside this virus family, in addition to its implications in transcription regulation and its likeliness as an antiviral target. |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
-モデル
モデル #1777 | ![]() タイプ: dummy / ダミー原子の半径: 1.75 A / カイ2乗値: 1.232 / P-value: 0.039236 ![]() |
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試料
![]() | 名称: Human respiratory syncytial virus (HRSV) M2–1 RNA-binding core domain 試料濃度: 4.50-9.00 |
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バッファ | 名称: 20 mM Tris–HCl, 300 mM NaCl, / pH: 7 |
要素 #963 | 名称: HRSV M2-1 / タイプ: protein / 記述: Human respiratory syncytial virus M2-1 / 分子量: 13.658 / 分子数: 1 / 由来: Human orthopneumovirus / 参照: UniProt: Q4KRW3 配列: ALGVVGVLES YIGSINNITK QSACVAMSKL LTELNSDDIK KLRDNEELNS PKIRVYNTVI SYIESNRKNN KQTIHLLKRL PADVLKKTIK NTLDIHKSIT INNPKELTVS DTNDHAKNND TT |
-実験情報
ビーム | 設備名称: PETRA III EMBL P12 / 地域: Hamburg / 国: Germany ![]() | |||||||||||||||||||||||||||||||||
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検出器 | 名称: Pilatus 2M | |||||||||||||||||||||||||||||||||
スキャン | 測定日: 2016年12月13日 / 保管温度: 10 °C / セル温度: 10 °C / 照射時間: 0.045 sec. / フレーム数: 20 / 単位: 1/nm /
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距離分布関数 P(R) |
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結果 |
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