SrasV1, Ncbi, Merge, bibRecord, 001440

Expression, purification and crystallization of the SARS-CoV macro domain.

Identifieur interne : 001440 ( Ncbi/Merge ); précédent : 001439; suivant : 001441

Expression, purification and crystallization of the SARS-CoV macro domain.

Auteurs : Hélène Malet [France] ; Karen Dalle ; Nicolas Brémond ; Fabienne Tocque ; Stéphanie Blangy ; Valérie Campanacci ; Bruno Coutard ; Sacha Grisel ; Julie Lichière ; Violaine Lantez ; Christian Cambillau ; Bruno Canard ; Marie Pierre Egloff

Source :

Acta crystallographica. Section F, Structural biology and crystallization communications [ 1744-3091 ] ; 2006.

RBID : pubmed:16582497

Descripteurs français

English descriptors

KwdEn :
- Cloning, Molecular, Crystallization, Peptide Fragments (chemistry), Peptide Fragments (isolation & purification), RNA Replicase (chemistry), RNA Replicase (genetics), RNA Replicase (isolation & purification), RNA Replicase (metabolism), Recombinant Proteins (chemistry), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), SARS Virus (enzymology), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (isolation & purification), Viral Nonstructural Proteins (metabolism), Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (isolation & purification), Viral Proteins (metabolism), X-Ray Diffraction.
MESH :
- chemical , chemistry : Peptide Fragments, RNA Replicase, Recombinant Proteins, Viral Nonstructural Proteins, Viral Proteins.
- chemical , genetics : RNA Replicase, Viral Nonstructural Proteins, Viral Proteins.
- chemical , isolation & purification : Peptide Fragments, RNA Replicase, Recombinant Proteins, Viral Nonstructural Proteins, Viral Proteins.
- chemical , metabolism : RNA Replicase, Recombinant Proteins, Viral Nonstructural Proteins, Viral Proteins.
- enzymology : SARS Virus.
- Cloning, Molecular, Crystallization, X-Ray Diffraction.

Abstract

Macro domains or X domains are found as modules of multidomain proteins, but can also constitute a protein on their own. Recently, biochemical and structural studies of cellular macro domains have been performed, showing that they are active as ADP-ribose-1''-phosphatases. Macro domains are also present in a number of positive-stranded RNA viruses, but their precise function in viral replication is still unknown. The major human pathogen severe acute respiratory syndrome coronavirus (SARS-CoV) encodes 16 non-structural proteins (nsps), one of which (nsp3) encompasses a macro domain. The SARS-CoV nsp3 gene region corresponding to amino acids 182-355 has been cloned, expressed in Escherichia coli, purified and crystallized. The crystals belong to space group P2(1), with unit-cell parameters a = 37.5, b = 55.6, c = 108.9 angstroms, beta = 91.4 degrees, and the asymmetric unit contains either two or three molecules. Both native and selenomethionine-labelled crystals diffract to 1.8 angstroms.

DOI: 10.1107/S1744309106009274
PubMed: 16582497

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 002291
to stream PubMed, to step Curation: 002291
to stream PubMed, to step Checkpoint: 002192

Links to Exploration step

pubmed:16582497

Le document en format XML

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<front><div type="abstract" xml:lang="en">Macro domains or X domains are found as modules of multidomain proteins, but can also constitute a protein on their own. Recently, biochemical and structural studies of cellular macro domains have been performed, showing that they are active as ADP-ribose-1''-phosphatases. Macro domains are also present in a number of positive-stranded RNA viruses, but their precise function in viral replication is still unknown. The major human pathogen severe acute respiratory syndrome coronavirus (SARS-CoV) encodes 16 non-structural proteins (nsps), one of which (nsp3) encompasses a macro domain. The SARS-CoV nsp3 gene region corresponding to amino acids 182-355 has been cloned, expressed in Escherichia coli, purified and crystallized. The crystals belong to space group P2(1), with unit-cell parameters a = 37.5, b = 55.6, c = 108.9 angstroms, beta = 91.4 degrees, and the asymmetric unit contains either two or three molecules. Both native and selenomethionine-labelled crystals diffract to 1.8 angstroms.</div>
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<Abstract><AbstractText>Macro domains or X domains are found as modules of multidomain proteins, but can also constitute a protein on their own. Recently, biochemical and structural studies of cellular macro domains have been performed, showing that they are active as ADP-ribose-1''-phosphatases. Macro domains are also present in a number of positive-stranded RNA viruses, but their precise function in viral replication is still unknown. The major human pathogen severe acute respiratory syndrome coronavirus (SARS-CoV) encodes 16 non-structural proteins (nsps), one of which (nsp3) encompasses a macro domain. The SARS-CoV nsp3 gene region corresponding to amino acids 182-355 has been cloned, expressed in Escherichia coli, purified and crystallized. The crystals belong to space group P2(1), with unit-cell parameters a = 37.5, b = 55.6, c = 108.9 angstroms, beta = 91.4 degrees, and the asymmetric unit contains either two or three molecules. Both native and selenomethionine-labelled crystals diffract to 1.8 angstroms.</AbstractText>
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<ReferenceList><Reference><Citation>J Virol. 2005 Oct;79(20):12721-31</Citation>
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Expression, purification and crystallization of the SARS-CoV macro domain.

Expression, purification and crystallization of the SARS-CoV macro domain.

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