- PDB-9l8t: The apo structure (State 1) of African Swine Fever Virus DNA poly... -
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基本情報
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データベース: PDB / ID: 9l8t
タイトル
The apo structure (State 1) of African Swine Fever Virus DNA polymerase
要素
DNA polymerase
キーワード
DNA BINDING PROTEIN / ASFV / DNA polymerase / Virus
機能・相同性
機能・相同性情報
viral DNA genome replication / DNA-directed DNA polymerase / DNA-directed DNA polymerase activity / DNA replication / nucleotide binding / DNA binding 類似検索 - 分子機能
: / DNA polymerase family B, thumb domain / DNA-directed DNA polymerase, family B, multifunctional domain / DNA-directed DNA polymerase, family B, conserved site / DNA polymerase family B signature. / DNA polymerase family B / DNA polymerase family B, exonuclease domain / DNA-directed DNA polymerase, family B, exonuclease domain / DNA polymerase, palm domain superfamily / DNA polymerase type-B family ...: / DNA polymerase family B, thumb domain / DNA-directed DNA polymerase, family B, multifunctional domain / DNA-directed DNA polymerase, family B, conserved site / DNA polymerase family B signature. / DNA polymerase family B / DNA polymerase family B, exonuclease domain / DNA-directed DNA polymerase, family B, exonuclease domain / DNA polymerase, palm domain superfamily / DNA polymerase type-B family / DNA-directed DNA polymerase, family B / Ribonuclease H superfamily / Ribonuclease H-like superfamily / DNA/RNA polymerase superfamily 類似検索 - ドメイン・相同性
National Natural Science Foundation of China (NSFC)
中国
引用
ジャーナル: iScience / 年: 2025 タイトル: Structural basis for DNA replication by the African swine fever virus polymerase. 著者: Ziwei Hu / Yongjie SunKang / Zhiheng Liu / Lihong Huang / Wenbao Qi / Renhong Yan / 要旨: African swine fever virus (ASFV) devastates swine herds and lacks widely available antivirals. We show that the ASFV DNA polymerase beta (Pol β; gene ) localizes to viral replication factories and ...African swine fever virus (ASFV) devastates swine herds and lacks widely available antivirals. We show that the ASFV DNA polymerase beta (Pol β; gene ) localizes to viral replication factories and is required for viral replication. Cryo-electron microscopy structures of Pol β in apo and double-stranded DNA (dsDNA)-bound states reveal pronounced conformational flexibility that enables transitions between functional states. Binding to dsDNA promotes higher-order oligomerization that is essential for catalytic activity, as demonstrated by structure-guided mutagenesis and biochemical assays. These findings define the structural basis of ASFV genome synthesis, highlight the functional significance of Pol β during viral replication, and provide a framework for polymerase-targeted antiviral discovery.
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2024年12月28日
登録サイト: PDBJ / 処理サイト: PDBC
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2025年12月31日
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