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TitleStructural and biochemical characterization of human Schlafen 5.
Journal, issue, pagesNucleic Acids Res, Vol. 50, Issue 2, Page 1147-1161, Year 2022
Publish dateJan 25, 2022
AuthorsFelix J Metzner / Elisabeth Huber / Karl-Peter Hopfner / Katja Lammens /
PubMed AbstractThe Schlafen family belongs to the interferon-stimulated genes and its members are involved in cell cycle regulation, T cell quiescence, inhibition of viral replication, DNA-repair and tRNA ...The Schlafen family belongs to the interferon-stimulated genes and its members are involved in cell cycle regulation, T cell quiescence, inhibition of viral replication, DNA-repair and tRNA processing. Here, we present the cryo-EM structure of full-length human Schlafen 5 (SLFN5) and the high-resolution crystal structure of the highly conserved N-terminal core domain. We show that the core domain does not resemble an ATPase-like fold and neither binds nor hydrolyzes ATP. SLFN5 binds tRNA as well as single- and double-stranded DNA, suggesting a potential role in transcriptional regulation. Unlike rat Slfn13 or human SLFN11, human SLFN5 did not cleave tRNA. Based on the structure, we identified two residues in proximity to the zinc finger motif that decreased DNA binding when mutated. These results indicate that Schlafen proteins have divergent enzymatic functions and provide a structural platform for future biochemical and genetic studies.
External linksNucleic Acids Res / PubMed:35037067 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.85 - 3.44 Å
Structure data

13581

7ppj

EMDB-13581, PDB-7ppj:
human SLFN5
Method: EM (single particle) / Resolution: 3.44 Å

PDB-6rr9:
DNA/RNA binding protein
Method: X-RAY DIFFRACTION / Resolution: 3.432 Å

PDB-7q3z:
DNA/RNA binding protein
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsDNA BINDING PROTEIN / Zinc-finger protein / RNA-binding / nucleotide binding protein antiviral linked to tumorigenesis transcription regulation

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