5CQQ

Crystal structure of the Drosophila Zeste DNA binding domain in complex with DNA

5CQQ の概要

• エントリーDOI: 10.2210/pdb5cqq/pdb
• 分子名称: Regulatory protein zeste, DNA (5'-D(*CP*TP*GP*TP*TP*TP*TP*CP*CP*AP*CP*TP*CP*GP*TP*TP*TP*TP*T)-3'), DNA (5'-D(*AP*AP*AP*AP*AP*CP*GP*AP*GP*TP*GP*GP*AP*AP*AP*AP*CP*AP*G)-3'), ... (4 entities in total)
• 機能のキーワード: complex, protein-dna interaction, tanscription factor, gene regulation, transcription-dna complex, transcription/dna
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• 細胞内の位置: Nucleus: P09956
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 43500.47

構造登録者

Gao, G.N.,Wang, M.,Yang, N.,Huang, Y.,Xu, R.M. (登録日: 2015-07-22, 公開日: 2015-11-04, 最終更新日: 2024-03-20)

主引用文献

Gao, G.N.,Wang, M.,Yang, N.,Huang, Y.,Xu, R.M.
Structure of Zeste-DNA Complex Reveals a New Modality of DNA Recognition by Homeodomain-Like Proteins
J.Mol.Biol., 427:3824-3833, 2015

PubMed Abstract: Drosophila Zeste is a DNA binding protein important for chromatin-targeted regulation of gene expression. It is best studied in the context of transvection-a mechanism of interallelic gene regulation involving paired chromosomes-and repression of the expression of white by Zeste mutants. Both of these functions depend on the DNA binding and self-association properties of Zeste, but the underlying structural basis remains unknown. Here we report the crystal structure of the DNA binding domain of Zeste in complex with a 19-bp DNA duplex containing the consensus recognition sequence motif. The structure reveals a helix-turn-helix Myb/homeodomain-like fold with the Zeste-specific insertion sequence forming a short helix and a long loop. Direct base contacts by the major groove binding helix principally account for the sequence-specific recognition, and backbone contacts via the Zeste-specific insertion are mainly responsible for the length requirement and the orientation of DNA. Our structural and biochemical characterizations of the DNA binding property of Zeste uncover an altered DNA binding modality of homeodomain-like proteins, and the structural information should facilitate the unraveling of the intricate mechanism of Zeste in regulation of gene expression.

PubMed: 26478222
DOI: 10.1016/j.jmb.2015.10.008

実験手法

X-RAY DIFFRACTION (3.1 Å)