5W2M

APOBEC3F Catalytic Domain Complex with a Single-Stranded DNA

5W2M の概要

• エントリーDOI: 10.2210/pdb5w2m/pdb
• 分子名称: DNA dC->dU-editing enzyme APOBEC-3F, DNA (5'-D(P*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3'), ZINC ION (3 entities in total)
• 機能のキーワード: apobec, dna binding protein
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Cytoplasm: Q8IUX4
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 183398.86

構造登録者

Fang, Y.,Xiao, X.,Li, S.-X.,Wolfe, A.,Chen, X.S. (登録日: 2017-06-06, 公開日: 2017-12-13, 最終更新日: 2024-10-16)

主引用文献

Fang, Y.,Xiao, X.,Li, S.X.,Wolfe, A.,Chen, X.S.
Molecular Interactions of a DNA Modifying Enzyme APOBEC3F Catalytic Domain with a Single-Stranded DNA.
J. Mol. Biol., 430:87-101, 2018

PubMed Abstract: The single-stranded DNA (ssDNA) cytidine deaminase APOBEC3F (A3F) deaminates cytosine (C) to uracil (U) and is a known restriction factor of HIV-1. Its C-terminal catalytic domain (CD2) alone is capable of binding single-stranded nucleic acids and is important for deamination. However, little is known about how the CD2 interacts with ssDNA. Here we report a crystal structure of A3F-CD2 in complex with a 10-nucleotide ssDNA composed of poly-thymine, which reveals a novel positively charged nucleic acid binding site distal to the active center that plays a key role in substrate DNA binding and catalytic activity. Lysine and tyrosine residues within this binding site interact with the ssDNA, and mutating these residues dramatically impairs both ssDNA binding and catalytic activity. This binding site is not conserved in APOBEC3G (A3G), which may explain differences in ssDNA-binding characteristics between A3F-CD2 and A3G-CD2. In addition, we observed an alternative Zn-coordination conformation around the active center. These findings reveal the structural relationships between nucleic acid interactions and catalytic activity of A3F.

PubMed: 29191651
DOI: 10.1016/j.jmb.2017.11.007

実験手法

X-RAY DIFFRACTION (3.7 Å)