Serveur d'exploration SRAS

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Insights into SARS-CoV transcription and replication from the structure of the nsp7–nsp8 hexadecamer

Identifieur interne : 004B73 ( Main/Exploration ); précédent : 004B72; suivant : 004B74

Insights into SARS-CoV transcription and replication from the structure of the nsp7–nsp8 hexadecamer

Auteurs : Yujia Zhai [République populaire de Chine] ; Fei Sun [République populaire de Chine] ; Xuemei Li [République populaire de Chine] ; Hai Pang [République populaire de Chine] ; Xiaoling Xu [République populaire de Chine] ; Mark Bartlam [République populaire de Chine] ; Zihe Rao [République populaire de Chine]

Source :

RBID : ISTEX:90054B6A9F2036EE747938F20BD3A1782FF5D6C0

Descripteurs français

English descriptors

Abstract

Coronavirus replication and transcription machinery involves multiple virus-encoded nonstructural proteins (nsp). We report the crystal structure of the hexadecameric nsp7–nsp8 supercomplex from the severe acute respiratory syndrome coronavirus at 2.4-Å resolution. nsp8 has a novel 'golf-club' fold with two conformations. The supercomplex is a unique hollow, cylinder-like structure assembled from eight copies of nsp8 and held tightly together by eight copies of nsp7. With an internal diameter of ∼30 Å, the central channel has dimensions and positive electrostatic properties favorable for nucleic acid binding, implying that its role is to confer processivity on RNA-dependent RNA polymerase.

Url:
DOI: 10.1038/nsmb999


Affiliations:


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<div type="abstract" xml:lang="eng">Coronavirus replication and transcription machinery involves multiple virus-encoded nonstructural proteins (nsp). We report the crystal structure of the hexadecameric nsp7–nsp8 supercomplex from the severe acute respiratory syndrome coronavirus at 2.4-Å resolution. nsp8 has a novel 'golf-club' fold with two conformations. The supercomplex is a unique hollow, cylinder-like structure assembled from eight copies of nsp8 and held tightly together by eight copies of nsp7. With an internal diameter of ∼30 Å, the central channel has dimensions and positive electrostatic properties favorable for nucleic acid binding, implying that its role is to confer processivity on RNA-dependent RNA polymerase.</div>
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