5cqq

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

spinqualitylabelsall models 5cqq, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5cqq is a 6 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ZEST_DROME Involved in transvection phenomena (= synapsis-dependent gene expression), where the synaptic pairing of chromosomes carrying genes with which zeste interacts influences the expression of these genes. Zeste binds to DNA and stimulates transcription from a nearby promoter. Publication Abstract from PubMed 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. Structure of Zeste-DNA Complex Reveals a New Modality of DNA Recognition by Homeodomain-Like Proteins.,Gao GN, Wang M, Yang N, Huang Y, Xu RM J Mol Biol. 2015 Dec 4;427(24):3824-33. doi: 10.1016/j.jmb.2015.10.008. Epub 2015, Oct 21. PMID:26478222 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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