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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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
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author Piotrowski, Yvonne
Hansen, Guido
Boomaars-van der Zanden, A Linda
Snijder, Eric J
Gorbalenya, Alexander E
Hilgenfeld, Rolf
author_facet Piotrowski, Yvonne
Hansen, Guido
Boomaars-van der Zanden, A Linda
Snijder, Eric J
Gorbalenya, Alexander E
Hilgenfeld, Rolf
author_sort Piotrowski, Yvonne
collection PubMed
description 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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spelling pubmed-27080382010-01-01 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 Piotrowski, Yvonne Hansen, Guido Boomaars-van der Zanden, A Linda Snijder, Eric J Gorbalenya, Alexander E Hilgenfeld, Rolf Protein Sci Accelerated Communication 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. Wiley Subscription Services, Inc., A Wiley Company 2009-01 2008-12-02 /pmc/articles/PMC2708038/ /pubmed/19177346 http://dx.doi.org/10.1002/pro.15 Text en Copyright © 2009 The Protein Society
spellingShingle Accelerated Communication
Piotrowski, Yvonne
Hansen, Guido
Boomaars-van der Zanden, A Linda
Snijder, Eric J
Gorbalenya, Alexander E
Hilgenfeld, Rolf
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
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
title_full 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
title_fullStr 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
title_full_unstemmed 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
title_short 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
title_sort 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
topic Accelerated Communication
url 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
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