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The crystal structure of the human smacovirus 1 Rep domain.
Limón, Lidia K; Shi, Ke; Dao, Amy; Rugloski, Jacob; Tompkins, Kassidy J; Aihara, Hideki; Gordon, Wendy R; Evans, Robert L.
Afiliação
  • Limón LK; Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
  • Shi K; Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
  • Dao A; Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
  • Rugloski J; Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
  • Tompkins KJ; Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
  • Aihara H; Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
  • Gordon WR; Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
  • Evans RL; Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Acta Crystallogr F Struct Biol Commun ; 79(Pt 12): 295-300, 2023 Dec 01.
Article em En | MEDLINE | ID: mdl-38051309
ABSTRACT
Replication initiator proteins (Reps) from the HUH endonuclease family process specific single-stranded DNA sequences to initiate rolling-circle replication in viruses. Here, the first crystal structure of the apo state of a Rep domain from the smacovirus family is reported. The structure of the human smacovirus 1 Rep domain was obtained at 1.33 Šresolution and represents an expansion of the HUH endonuclease superfamily, allowing greater diversity in bioconjugation-tag applications.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: DNA de Cadeia Simples / Endonucleases Limite: Humans Idioma: En Revista: Acta Crystallogr F Struct Biol Commun Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Estados Unidos
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: DNA de Cadeia Simples / Endonucleases Limite: Humans Idioma: En Revista: Acta Crystallogr F Struct Biol Commun Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Estados Unidos