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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
Yvonne Piotrowski 1, Guido Hansen 1, A. Linda Boomaars-van der Zanden 2, Eric J. Snijder 2, Alexander E. Gorbalenya 2, Rolf Hilgenfeld 1 3 *
1Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany
2Molecular Virology Laboratory, Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, The Netherlands
3Laboratory for Structural Biology of Infection and Inflammation, c/o DESY, Building 22a, Notkestr. 85, 22603 Hamburg, Germany
email: Rolf Hilgenfeld (hilgenfeld@biochem.uni-luebeck.de)

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

Funded by:
 European Commission; Grant Number: LSHG-CT-2004-511960 VIZIER, SP22-CT-2004-003831 SEPSDA
 Schleswig-Holstein Innovation Fund
 Sino-German Center for the Promotion of Research, Beijing

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.
Received: 2 October 2008; Revised: 14 October 2008; Accepted: 15 October 2008

Digital Object Identifier (DOI)

10.1002/pro.15  About DOI