Accelerated Communication

You have full text access to this OnlineOpen article

Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property

  1. Yvonne Piotrowski1,
  2. Guido Hansen1,
  3. A. Linda Boomaars-van der Zanden2,
  4. Eric J. Snijder2,
  5. Alexander E. Gorbalenya2,
  6. Rolf Hilgenfeld1,3,*

Article first published online: 2 DEC 2008

DOI: 10.1002/pro.15

Issue

Protein Science

Protein Science

Volume 18, Issue 1, pages 6–16, January 2009

Additional Information

How to Cite

Piotrowski, Y., Hansen, G., Boomaars-van der Zanden, A. L., Snijder, E. J., Gorbalenya, A. E. and Hilgenfeld, R. (2009), Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property. Protein Science, 18: 6–16. doi: 10.1002/pro.15

Author Information

  1. 1

    Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany

  2. 2

    Molecular Virology Laboratory, Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, The Netherlands

  3. 3

    Laboratory for Structural Biology of Infection and Inflammation, c/o DESY, Building 22a, Notkestr. 85, 22603 Hamburg, Germany

*Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany

Publication History

  1. Issue published online: 16 DEC 2008
  2. Article first published online: 2 DEC 2008
  3. Accepted manuscript online: 2 DEC 2008 12:00AM EST
  4. Manuscript Accepted: 15 OCT 2008
  5. Manuscript Revised: 14 OCT 2008
  6. Manuscript Received: 2 OCT 2008

Funded by

  • European Commission. Grant Numbers: LSHG-CT-2004-511960 VIZIER, SP22-CT-2004-003831 SEPSDA
  • Schleswig-Holstein Innovation Fund
  • Sino-German Center for the Promotion of Research, Beijing

SEARCH

SEARCH BY CITATION

ARTICLE TOOLS

View Full Article (HTML) Get PDF (345K)

Keywords:

  • X-domain;
  • macrodomain;
  • nonstructural protein 3;
  • coronavirus;
  • SARS;
  • ADP-ribose;
  • X-ray structure;
  • ADP-ribose-1″-phosphate phosphatase

Abstract

The polyproteins of coronaviruses are cleaved by viral proteases into at least 15 nonstructural proteins (Nsps). Consisting of five domains, Nsp3 is the largest of these (180–210 kDa). Among these domains, the so-called X-domain is believed to act as ADP-ribose-1″-phosphate phosphatase or to bind poly(ADP-ribose). However, here we show that the X-domain of Infectious Bronchitis Virus (strain Beaudette), a Group-3 coronavirus, fails to bind ADP-ribose. This is explained on the basis of the crystal structure of the protein, determined at two different pH values. For comparison, we also describe the crystal structure of the homologous X-domain from Human Coronavirus 229E, a Group-1 coronavirus, which does bind ADP-ribose.

View Full Article (HTML) Get PDF (345K)