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; Guido Hansen; A. Linda Boomaars-van Der Zanden; Eric J. Snijder; Alexander E. Gorbalenya; Rolf Hilgenfeld

doi:10.1002/pro.15

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, Guido Hansen, A. Linda Boomaars-van Der Zanden, Eric J. Snijder, Alexander E. Gorbalenya, Rolf Hilgenfeld^*

^*Corresponding author for this work

Institute of Biochemistry

27 Citations (Scopus)

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. Published by Wiley-Blackwell.

Original language	English
Journal	Protein Science
Volume	18
Issue number	1
Pages (from-to)	6-16
Number of pages	11
ISSN	0961-8368
DOIs	https://doi.org/10.1002/pro.15
Publication status	Published - 01.01.2009

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Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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title = "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",

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. Published by Wiley-Blackwell.",

author = "Yvonne Piotrowski and Guido Hansen and {Boomaars-van Der Zanden}, {A. Linda} and Snijder, {Eric J.} and Gorbalenya, {Alexander E.} and Rolf Hilgenfeld",

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AU - Piotrowski, Yvonne

AU - Hansen, Guido

AU - Boomaars-van Der Zanden, A. Linda

AU - Snijder, Eric J.

AU - Gorbalenya, Alexander E.

AU - Hilgenfeld, Rolf

PY - 2009/1/1

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N2 - 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. Published by Wiley-Blackwell.

AB - 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. Published by Wiley-Blackwell.

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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

Abstract

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