7PPJ

human SLFN5

7PPJ の概要

• エントリーDOI: 10.2210/pdb7ppj/pdb
• 関連するPDBエントリー: 6RR9
• EMDBエントリー: 13581
• 分子名称: Schlafen family member 5, ZINC ION (2 entities in total)
• 機能のキーワード: nucleotide binding protein antiviral linked to tumorigenesis transcription regulation, dna binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 104485.43

構造登録者

Lammens, K.,Metzner, F.J. (登録日: 2021-09-14, 公開日: 2022-01-26, 最終更新日: 2024-07-17)

主引用文献

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

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: 35037067
DOI: 10.1093/nar/gkab1278

実験手法

ELECTRON MICROSCOPY (3.44 Å)