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Journal of Virology, January 2009, p. 1083-1092, Vol. 83, No. 2
0022-538X/09/$08.00+0     doi:10.1128/JVI.01862-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Crystal Structures of Two Coronavirus ADP-Ribose-1''-Monophosphatases and Their Complexes with ADP-Ribose: a Systematic Structural Analysis of the Viral ADRP Domain{triangledown}

Yuanyuan Xu,1 Le Cong,1 Cheng Chen,1 Lei Wei,1 Qi Zhao,1 Xiaoling Xu,1 Yanlin Ma,2 Mark Bartlam,3 and Zihe Rao1,2,3*

Laboratory of Structural Biology, Tsinghua University, Beijing 100084, China,1 National Laboratory of Biomacromolecules, Institute of Biophysics (IBP), Chinese Academy of Sciences, Beijing 100101, China,2 College of Life Sciences and Tianjin State Laboratory of Protein Science, Nankai University, Tianjin 300071, China3

Received 4 September 2008/ Accepted 22 October 2008

The coronaviruses are a large family of plus-strand RNA viruses that cause a wide variety of diseases both in humans and in other organisms. The coronaviruses are composed of three main lineages and have a complex organization of nonstructural proteins (nsp's). In the coronavirus, nsp3 resides a domain with the macroH2A-like fold and ADP-ribose-1"-monophosphatase (ADRP) activity, which is proposed to play a regulatory role in the replication process. However, the significance of this domain for the coronaviruses is still poorly understood due to the lack of structural information from different lineages. We have determined the crystal structures of two viral ADRP domains, from the group I human coronavirus 229E and the group III avian infectious bronchitis virus, as well as their respective complexes with ADP-ribose. The structures were individually solved to elucidate the structural similarities and differences of the ADRP domains among various coronavirus species. The active-site residues responsible for mediating ADRP activity were found to be highly conserved in terms of both sequence alignment and structural superposition, whereas the substrate binding pocket exhibited variations in structure but not in sequence. Together with data from a previous analysis of the ADRP domain from the group II severe acute respiratory syndrome coronavirus and from other related functional studies of ADRP domains, a systematic structural analysis of the coronavirus ADRP domains was realized for the first time to provide a structural basis for the function of this domain in the coronavirus replication process.

* Corresponding author. Mailing address: Laboratory of Structural Biology, Life Sciences Building, Tsinghua University, Beijing 100084, China. Phone: 86 10 62771493. Fax: 86 10 62773145. E-mail: raozh{at}xtal.tsinghua.edu.cn

{triangledown} Published ahead of print on 5 November 2008.

Journal of Virology, January 2009, p. 1083-1092, Vol. 83, No. 2
0022-538X/09/$08.00+0     doi:10.1128/JVI.01862-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



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