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Crystal structure of an avian influenza polymerase PAN reveals an endonuclease active site

Author

Listed:
  • Puwei Yuan

    (National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China)

  • Mark Bartlam

    (College of Life Sciences and Tianjin Key Laboratory of Protein Science, Nankai University)

  • Zhiyong Lou

    (Laboratory of Structural Biology, Tsinghua University)

  • Shoudeng Chen

    (National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China)

  • Jie Zhou

    (National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China)

  • Xiaojing He

    (National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China)

  • Zongyang Lv

    (National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China)

  • Ruowen Ge

    (National University of Singapore)

  • Xuemei Li

    (National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
    Laboratory of Structural Biology, Tsinghua University)

  • Tao Deng

    (College of Life Sciences and Tianjin Key Laboratory of Protein Science, Nankai University
    Sir William Dunn School of Pathology, University of Oxford)

  • Ervin Fodor

    (Sir William Dunn School of Pathology, University of Oxford)

  • Zihe Rao

    (National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
    College of Life Sciences and Tianjin Key Laboratory of Protein Science, Nankai University
    Laboratory of Structural Biology, Tsinghua University)

  • Yingfang Liu

    (National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China)

Abstract

Avian flu virus polymerase The influenza virus RNA-dependent RNA polymerase, which contains three subunits (PA, PB1 and PB2), directs the replication and transcription of viral RNA inside the nuclei of infected cells. Two groups now report the crystal structure of the N terminus of the PA subunit of avian influenza virus. Structural comparison and mutational analysis show that the PA subunit contains an endonucleolytic cleavage site, an activity previously suspected to reside on the PB1 subunit. The PA endonuclease active site is highly conserved across influenza strains, making it a promising potential target for new anti-influenza drugs.

Suggested Citation

  • Puwei Yuan & Mark Bartlam & Zhiyong Lou & Shoudeng Chen & Jie Zhou & Xiaojing He & Zongyang Lv & Ruowen Ge & Xuemei Li & Tao Deng & Ervin Fodor & Zihe Rao & Yingfang Liu, 2009. "Crystal structure of an avian influenza polymerase PAN reveals an endonuclease active site," Nature, Nature, vol. 458(7240), pages 909-913, April.
    • Handle: RePEc:nat:nature:v:458:y:2009:i:7240:d:10.1038_nature07720
    DOI: 10.1038/nature07720
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