6X91

Crystal structure of MBP-fused human APOBEC1

6X91 の概要

• エントリーDOI: 10.2210/pdb6x91/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltodextrin-binding protein, C->U-editing enzyme APOBEC-1 chimera, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ZINC ION, ... (4 entities in total)
• 機能のキーワード: apobec, rna editing, deamination, metalloenzyme, hydrolase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 542997.84

構造登録者

Wolfe, A.D.,Li, S.-X.,Chen, X.S. (登録日: 2020-06-02, 公開日: 2020-12-09, 最終更新日: 2023-10-18)

主引用文献

Wolfe, A.D.,Li, S.,Goedderz, C.,Chen, X.S.
The structure of APOBEC1 and insights into its RNA and DNA substrate selectivity.
NAR Cancer, 2:zcaa027-zcaa027, 2020

PubMed Abstract: APOBEC1 (APO1), a member of AID/APOBEC nucleic acid cytosine deaminase family, can edit apolipoprotein B mRNA to regulate cholesterol metabolism. This APO1 RNA editing activity requires a cellular cofactor to achieve tight regulation. However, no cofactors are required for deamination on DNA by APO1 and other AID/APOBEC members, and aberrant deamination on genomic DNA by AID/APOBEC deaminases has been linked to cancer. Here, we present the crystal structure of APO1, which reveals a typical APOBEC deaminase core structure, plus a unique well-folded C-terminal domain that is highly hydrophobic. This APO1 C-terminal hydrophobic domain (A1HD) interacts to form a stable dimer mainly through hydrophobic interactions within the dimer interface to create a four-stranded β-sheet positively charged surface. Structure-guided mutagenesis within this and other regions of APO1 clarified the importance of the A1HD in directing RNA and cofactor interactions, providing insights into the structural basis of selectivity on DNA or RNA substrates.

PubMed: 33094286
DOI: 10.1093/narcan/zcaa027

実験手法

X-RAY DIFFRACTION (3.51 Å)