5CQQ

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

Summary for 5CQQ

• Entry DOI: 10.2210/pdb5cqq/pdb
• Descriptor: 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)
• Functional Keywords: complex, protein-dna interaction, tanscription factor, gene regulation, transcription-dna complex, transcription/dna
• Biological source: Drosophila melanogaster (Fruit fly); More
• Cellular location: Nucleus: P09956
• Total number of polymer chains: 6
• Total formula weight: 43500.47

Authors

Gao, G.N.,Wang, M.,Yang, N.,Huang, Y.,Xu, R.M. (deposition date: 2015-07-22, release date: 2015-11-04, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.1 Å)