SASDDE3: Human respiratory syncytial virus (HRSV) M2–1 RNA-binding core domain

基本情報

• 登録情報: データベース: SASBDB / ID: SASDDE3

試料

Human respiratory syncytial virus (HRSV) M2–1 RNA-binding core domain

• Human respiratory syncytial virus M2-1 (protein), HRSV M2-1, Human orthopneumovirus

機能・相同性

分子機能:

regulation of viral transcription / symbiont-mediated activation of host NF-kappaB cascade / viral transcription / translation elongation factor activity / transcription antitermination / virion component / host cell cytoplasm / structural constituent of virion / host cell nucleus / RNA binding / metal ion binding

ドメイン・相同性:

Pneumovirus matrix 2-1 / Pneumovirus matrix protein 2 (M2) / Zinc finger, CCCH-type superfamily / zinc finger / Zinc finger, CCCH-type / Zinc finger C3H1-type profile.

構成要素:

Protein M2-1

• 生物種: Human orthopneumovirus (ウイルス)
• 引用: ジャーナル: Acta Crystallogr F Struct Biol Commun / 年: 2018; 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, 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.

登録者

• Yasser Almeida (University of Hamburg, Hamburg, Germany)

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; Omokage検索でこの集合体の類似形状データを探す (詳細)

試料

• 試料: 名称: Human respiratory syncytial virus (HRSV) M2–1 RNA-binding core domain; 試料濃度: 4.50-9.00
• 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 / 線源: X-ray synchrotron / 波長: 0.124 Å / スペクトロメータ・検出器間距離: 3 mm
• 検出器: 名称: Pilatus 2M

スキャン

タイトル: Human respiratory syncytial virus (HRSV) M 2–1 RNA-binding core domain
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 /

	Min	Max
Q	0.0195	5.0075

距離分布関数 P(R)

ソフトウェア P(R): GNOM 5.0 / ポイント数: 1325 /

	Min	Max
Q	0.225008	3.85364
P(R) point	1	1325
R	0	7.9

結果

カーブのタイプ: single_conc /

	実験値	Porod
分子量	15 kDa	15 kDa
体積	-	2.64 nm3

	P(R)	P(R) error	Guinier	Guinier error
前方散乱 I0	3865	5.1	3828.08	3.24
慣性半径, Rg	2.14 nm	0.005	2.03 nm	-

	Min	Max
D	-	7.9
Guinier point	63	228