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

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 po...

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Detalles Bibliográficos
Autores principales: Piotrowski, Yvonne, Hansen, Guido, Boomaars-van der Zanden, A Linda, Snijder, Eric J, Gorbalenya, Alexander E, Hilgenfeld, Rolf
Formato: Texto
Lenguaje:English
Publicado: Wiley Subscription Services, Inc., A Wiley Company 2009
Materias:
Accelerated Communication
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2708038/
https://www.ncbi.nlm.nih.gov/pubmed/19177346
http://dx.doi.org/10.1002/pro.15
Descripción
Sumario: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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