+データを開く
-基本情報
登録情報 | データベース: SASBDB / ID: SASDAQ8 |
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試料 | kLANA mutant dimer-tetramer mixture
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機能・相同性 | : / Protein LANA1-like, DNA-binding domain / Epstein Barr virus nuclear antigen-1, DNA-binding domain superfamily / symbiont-mediated suppression of host NF-kappaB cascade / viral life cycle / host cell nucleus / DNA binding / Protein LANA1 機能・相同性情報 |
生物種 | Human herpesvirus 8 (ヘルペスウイルス) |
引用 | ジャーナル: Nucleic Acids Res / 年: 2015 タイトル: KSHV but not MHV-68 LANA induces a strong bend upon binding to terminal repeat viral DNA. 著者: Rajesh Ponnusamy / Maxim V Petoukhov / Bruno Correia / Tania F Custodio / Franceline Juillard / Min Tan / Marta Pires de Miranda / Maria A Carrondo / J Pedro Simas / Kenneth M Kaye / Dmitri I ...著者: Rajesh Ponnusamy / Maxim V Petoukhov / Bruno Correia / Tania F Custodio / Franceline Juillard / Min Tan / Marta Pires de Miranda / Maria A Carrondo / J Pedro Simas / Kenneth M Kaye / Dmitri I Svergun / Colin E McVey / 要旨: Latency-associated nuclear antigen (LANA) is central to episomal tethering, replication and transcriptional regulation of γ2-herpesviruses. LANA binds cooperatively to the terminal repeat (TR) ...Latency-associated nuclear antigen (LANA) is central to episomal tethering, replication and transcriptional regulation of γ2-herpesviruses. LANA binds cooperatively to the terminal repeat (TR) region of the viral episome via adjacent LANA binding sites (LBS), but the molecular mechanism by which LANA assembles on the TR remains elusive. We show that KSHV LANA and MHV-68 LANA proteins bind LBS DNA using strikingly different modes. Solution structure of LANA complexes revealed that while kLANA tetramer is intrinsically bent both in the free and bound state to LBS1-2 DNA, mLANA oligomers instead adopt a rigid linear conformation. In addition, we report a novel non-ring kLANA structure that displays more flexibility at its assembly interface than previously demonstrated. We identified a hydrophobic pivot point located at the dimer-dimer assembly interface, which gives rotational freedom for kLANA to adopt variable conformations to accommodate both LBS1-2 and LBS2-1-3 DNA. Alterations in the arrangement of LBS within TR or at the tetramer assembly interface have a drastic effect on the ability of kLANA binding. We also show kLANA and mLANA DNA binding functions can be reciprocated. Although KSHV and MHV-68 are closely related, the findings provide new insights into how the structure, oligomerization, and DNA binding of LANA have evolved differently to assemble on the TR DNA. |
登録者 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-モデル
モデル #335 | タイプ: mix / ソフトウェア: oligomer / ダミー原子の半径: 1.90 A / カイ2乗値: 0.83 Omokage検索でこの集合体の類似形状データを探す (詳細) |
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モデル #336 | タイプ: mix / ソフトウェア: oligomer / ダミー原子の半径: 1.90 A / カイ2乗値: 0.83 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: kLANA mutant dimer-tetramer mixture / 試料濃度: 2.5 mg/ml / Entity id: 196 / 197 |
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バッファ | 名称: 25 mM Na/K Phosphate / pH: 7.5 |
要素 #196 | 名称: kLANA mutant K1109E / タイプ: protein / 記述: ORF73 tetramer / 分子量: 15.759 / 分子数: 4 / 由来: Human herpesvirus 8 / 参照: UniProt: Q9QR71 配列: SHPRYQQPPV PYRQIDDCPA KARPQHIFYR RFLGKDGRRD PKCQWKFAVI FWGNDPYGLK KLSQAFQFGG VKAGPVSCLP HPGPDQSPIT YCVYVYCQNK DTSKKVQMAR LAWEASHPLA GNLQSSIVKF KKPLPLTQ |
要素 #197 | 名称: kLANA mutant K1109E / タイプ: protein / 記述: ORF73 dimer / 分子量: 15.759 / 分子数: 2 / 由来: Human herpesvirus 8 / 参照: UniProt: Q9QR71 配列: SHPRYQQPPV PYRQIDDCPA KARPQHIFYR RFLGKDGRRD PKCQWKFAVI FWGNDPYGLK KLSQAFQFGG VKAGPVSCLP HPGPDQSPIT YCVYVYCQNK DTSKKVQMAR LAWEASHPLA GNLQSSIVKF KKPLPLTQ |
-実験情報
ビーム | 設備名称: ESRF BM29 / 地域: Grenoble / 国: France / 線源: X-ray synchrotron / 波長: 0.93 Å / スペクトロメータ・検出器間距離: 2.43 mm | |||||||||||||||||||||
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検出器 | 名称: Pilatus 1M | |||||||||||||||||||||
スキャン | タイトル: kLANA mutant mixture / 測定日: 2014年6月21日 / 単位: 1/nm /
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距離分布関数 P(R) | ソフトウェア P(R): GNOM 5.0 / ポイント数: 491 /
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結果 | D max: 9.5 / カーブのタイプ: single_conc コメント: Study of oligomeric states of mLANA and kLANA and their complexes with DNA
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