SrasV1, PubMed, Checkpoint, bibRecord, 000E37

Crystallization and preliminary X-ray crystallographic analysis of a nonstructural protein 15 mutant from Human coronavirus 229E.

Identifieur interne : 000E37 ( PubMed/Checkpoint ); précédent : 000E36; suivant : 000E38

Crystallization and preliminary X-ray crystallographic analysis of a nonstructural protein 15 mutant from Human coronavirus 229E.

Auteurs : Tong Huo [République populaire de Chine] ; Xiang Liu [République populaire de Chine]

Source :

Acta crystallographica. Section F, Structural biology communications [ 2053-230X ] ; 2015.

RBID : pubmed:26323302

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Chromatography, Gel, Coronavirus 229E, Human (chemistry), Crystallization, Crystallography, X-Ray, Electrophoresis, Polyacrylamide Gel, Molecular Sequence Data, Molecular Weight, Mutant Proteins (chemistry), Ultracentrifugation, Viral Nonstructural Proteins (chemistry).
MESH :
- chemical , chemistry : Mutant Proteins, Viral Nonstructural Proteins.
- chemistry : Coronavirus 229E, Human.
- Amino Acid Sequence, Chromatography, Gel, Crystallization, Crystallography, X-Ray, Electrophoresis, Polyacrylamide Gel, Molecular Sequence Data, Molecular Weight, Ultracentrifugation.

Abstract

Nonstructural protein 15 (nsp15), also called endoribonuclease, is a gene product of open reading frame 1b (ORF 1b) in coronaviruses. It is an important enzyme in the transcription/replication process involved in discontinuous negative-strand RNA synthesis. In this work, mutants of nsp15 from Human coronavirus 229E (HCoV-229E) were made based on structural analysis of the homologous nsp15s in Severe acute respiratory syndrome coronavirus (SARS-CoV) and Mouse hepatitis virus (MHV). The I26A/N52A mutant of nsp15 was overexpressed, purified and crystallized, and this mutant led to a trimeric form rather than hexamers or monomers. Crystals of trimeric nsp15 were obtained by the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitant and diffracted to 2.5 Å resolution. The crystals belonged to space group C2221, with unit-cell parameters a = 85.9, b = 137.5, c = 423.1 Å, α = β = γ = 90°.

DOI: 10.1107/S2053230X15007359
PubMed: 26323302

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<front><div type="abstract" xml:lang="en">Nonstructural protein 15 (nsp15), also called endoribonuclease, is a gene product of open reading frame 1b (ORF 1b) in coronaviruses. It is an important enzyme in the transcription/replication process involved in discontinuous negative-strand RNA synthesis. In this work, mutants of nsp15 from Human coronavirus 229E (HCoV-229E) were made based on structural analysis of the homologous nsp15s in Severe acute respiratory syndrome coronavirus (SARS-CoV) and Mouse hepatitis virus (MHV). The I26A/N52A mutant of nsp15 was overexpressed, purified and crystallized, and this mutant led to a trimeric form rather than hexamers or monomers. Crystals of trimeric nsp15 were obtained by the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitant and diffracted to 2.5 Å resolution. The crystals belonged to space group C2221, with unit-cell parameters a = 85.9, b = 137.5, c = 423.1 Å, α = β = γ = 90°. </div>
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Crystallization and preliminary X-ray crystallographic analysis of a nonstructural protein 15 mutant from Human coronavirus 229E.

Crystallization and preliminary X-ray crystallographic analysis of a nonstructural protein 15 mutant from Human coronavirus 229E.

Source :

Descripteurs français

English descriptors

Abstract

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

Links to Exploration step

Le document en format XML

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