An iron-sulfur cluster in the zinc-binding domain of the SARS-CoV-2 helicase modulates its RNA-binding and -unwinding activities.

Maio, Nunziata; Raza, Md Kausar; Li, Yan; Zhang, De-Liang; Bollinger, J Martin; Krebs, Carsten; Rouault, Tracey A

Maio, Nunziata; Raza, Md Kausar; Li, Yan; Zhang, De-Liang; Bollinger, J Martin; Krebs, Carsten; Rouault, Tracey A.

Afiliação

Maio N; Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH, Bethesda, MD 20892.
Raza MK; Department of Chemistry, The Pennsylvania State University, University Park, PA 16802.
Li Y; National Institute of Neurological Disorders and Stroke, NIH, Proteomics Core Facility, Bethesda, MD 20892.
Zhang DL; Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH, Bethesda, MD 20892.
Bollinger JM; Department of Chemistry, The Pennsylvania State University, University Park, PA 16802.
Krebs C; Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802.
Rouault TA; Department of Chemistry, The Pennsylvania State University, University Park, PA 16802.

Proc Natl Acad Sci U S A ; 120(33): e2303860120, 2023 08 15.

Article em En | MEDLINE | ID: mdl-37552760

Assuntos

COVID-19; SARS-CoV-2; Humanos; SARS-CoV-2/genética; Tratamento Farmacológico da COVID-19; DNA Helicases/metabolismo; RNA; Enxofre; Proteínas não Estruturais Virais/metabolismo; RNA Helicases/genética

Palavras-chave

SARS-CoV-2; iron-sulfur clusters; nsp13; viral helicase

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: SARS-CoV-2 / COVID-19 Limite: Humans Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2023 Tipo de documento: Article

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