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

Puwei Yuan, Mark Bartlam, Zhiyong Lou, Shoudeng Chen, Jie Zhou, Xiaojing He, Zongyang Lv, Ruowen Ge, Xuemei Li, Tao Deng, Ervin Fodor, Zihe Rao () and Yingfang Liu ()
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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
Tao Deng: College of Life Sciences and Tianjin Key Laboratory of Protein Science, Nankai University
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
Yingfang Liu: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China

Nature, 2009, vol. 458, issue 7240, 909-913

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.

Date: 2009
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DOI: 10.1038/nature07720

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