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5cqq

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==Crystal structure of the Drosophila Zeste DNA binding domain in complex with DNA==
==Crystal structure of the Drosophila Zeste DNA binding domain in complex with DNA==
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<StructureSection load='5cqq' size='340' side='right' caption='[[5cqq]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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<StructureSection load='5cqq' size='340' side='right'caption='[[5cqq]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5cqq]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CQQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CQQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5cqq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CQQ FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5cqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cqq OCA], [http://pdbe.org/5cqq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cqq RCSB], [http://www.ebi.ac.uk/pdbsum/5cqq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cqq ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5cqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cqq OCA], [https://pdbe.org/5cqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cqq RCSB], [https://www.ebi.ac.uk/pdbsum/5cqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cqq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ZEST_DROME 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.
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[https://www.uniprot.org/uniprot/ZEST_DROME 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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:26478222</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5cqq" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Gao, G N]]
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[[Category: Drosophila melanogaster]]
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[[Category: Huang, Y]]
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[[Category: Large Structures]]
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[[Category: Wang, M]]
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[[Category: Gao GN]]
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[[Category: Xu, R M]]
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[[Category: Huang Y]]
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[[Category: Yang, N]]
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[[Category: Wang M]]
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[[Category: Complex]]
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[[Category: Xu RM]]
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[[Category: Gene regulation]]
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[[Category: Yang N]]
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[[Category: Protein-dna interaction]]
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[[Category: Tanscription factor]]
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[[Category: Transcription-dna complex]]
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Current revision

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

PDB ID 5cqq

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