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Structure of the error-prone DNA ligase of African swine fever virus identifies critical active site residues

Author

Listed:
  • Yiqing Chen

    (Fudan University)

  • Hehua Liu

    (Fudan University
    Fudan University)

  • Chun Yang

    (Fudan University)

  • Yanqing Gao

    (Fudan University)

  • Xiang Yu

    (Fudan University
    Fudan University)

  • Xi Chen

    (Fudan University)

  • Ruixue Cui

    (Fudan University)

  • Lina Zheng

    (Fudan University)

  • Suhua Li

    (Fudan University)

  • Xuhang Li

    (Fudan University)

  • Jinbiao Ma

    (Fudan University)

  • Zhen Huang

    (Sichuan University
    Georgia State University)

  • Jixi Li

    (Fudan University
    Fudan University)

  • Jianhua Gan

    (Fudan University)

Abstract

African swine fever virus (ASFV) is contagious and can cause highly lethal disease in pigs. ASFV DNA ligase (AsfvLIG) is one of the most error-prone ligases identified to date; it catalyzes DNA joining reaction during DNA repair process of ASFV and plays important roles in mutagenesis of the viral genome. Here, we report four AsfvLIG:DNA complex structures and demonstrate that AsfvLIG has a unique N-terminal domain (NTD) that plays critical roles in substrate binding and catalytic complex assembly. In combination with mutagenesis, in vitro binding and catalytic assays, our study reveals that four unique active site residues (Asn153 and Leu211 of the AD domain; Leu402 and Gln403 of the OB domain) are crucial for the catalytic efficiency of AsfvLIG. These unique structural features can serve as potential targets for small molecule design, which could impair genome repair in ASFV and help combat this virus in the future.

Suggested Citation

  • Yiqing Chen & Hehua Liu & Chun Yang & Yanqing Gao & Xiang Yu & Xi Chen & Ruixue Cui & Lina Zheng & Suhua Li & Xuhang Li & Jinbiao Ma & Zhen Huang & Jixi Li & Jianhua Gan, 2019. "Structure of the error-prone DNA ligase of African swine fever virus identifies critical active site residues," Nature Communications, Nature, vol. 10(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-08296-w
    DOI: 10.1038/s41467-019-08296-w
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    Cited by:

    1. Qun Tang & Mitchell Gulkis & Robert McKenna & Melike Çağlayan, 2022. "Structures of LIG1 that engage with mutagenic mismatches inserted by polβ in base excision repair," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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