The crystal structure of the human smacovirus 1 Rep domain

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 hum...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2023-12, Vol.79 (12), p.295-300
Main Authors: Limón, Lidia K., Shi, Ke, Dao, Amy, Rugloski, Jacob, Tompkins, Kassidy J., Aihara, Hideki, Gordon, Wendy R., Evans, Robert L.
Format: Article
Language:English
Subjects:
bioconjugation
Crystal structure
Crystallography, X-Ray
Deoxyribonucleic acid
DNA
DNA, Single-Stranded
DNA, Viral - genetics
Endonuclease
Endonucleases - chemistry
Gene sequencing
HUH endonucleases
HUH‐tags
Humans
Nucleotide sequence
Rep domains
Replication
Research Communications
smacoviruses
ssDNA
Viruses
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Summary: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 Å resolution and represents an expansion of the HUH endonuclease superfamily, allowing greater diversity in bioconjugation‐tag applications. The structure of the human smacovirus 1 Rep domain was obtained at 1.33 Å resolution. This new HUH endonuclease offers a new ssDNA‐binding sequence specificity that will be exploited to increase orthogonality among Rep families.
ISSN:2053-230X
2053-230X
DOI:10.1107/S2053230X23009536