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 |
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| Authors: | Yvonne Piotrowski Guido Hansen A. Linda Boomaars‐van der Zanden Eric J. Snijder Alexander E. Gorbalenya Rolf Hilgenfeld |
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| Affiliation: | 1. Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany;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. Laboratory for Structural Biology of Infection and Inflammation, c/o DESY, Building 22a, Notkestr. 85, 22603 Hamburg, Germany |
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| 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. |
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| Keywords: | X‐domain macrodomain nonstructural protein 3 coronavirus SARS ADP‐ribose X‐ray structure ADP‐ribose‐1″ ‐phosphate phosphatase |
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