7PPJ
human SLFN5
Summary for 7PPJ
| Entry DOI | 10.2210/pdb7ppj/pdb |
| Related | 6RR9 |
| EMDB information | 13581 |
| Descriptor | Schlafen family member 5, ZINC ION (2 entities in total) |
| Functional Keywords | nucleotide binding protein antiviral linked to tumorigenesis transcription regulation, dna binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 104485.43 |
| Authors | Lammens, K.,Metzner, F.J. (deposition date: 2021-09-14, release date: 2022-01-26, Last modification date: 2024-07-17) |
| Primary citation | Metzner, F.J.,Huber, E.,Hopfner, K.P.,Lammens, K. Structural and biochemical characterization of human Schlafen 5. Nucleic Acids Res., 50:1147-1161, 2022 Cited by PubMed Abstract: 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. PubMed: 35037067DOI: 10.1093/nar/gkab1278 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.44 Å) |
Structure validation
Download full validation report
