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5ybd

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==X-ray structure of ETS domain of Ergp55 in complex with E74DNA==
==X-ray structure of ETS domain of Ergp55 in complex with E74DNA==
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<StructureSection load='5ybd' size='340' side='right' caption='[[5ybd]], [[Resolution|resolution]] 2.77&Aring;' scene=''>
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<StructureSection load='5ybd' size='340' side='right'caption='[[5ybd]], [[Resolution|resolution]] 2.77&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ybd]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YBD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YBD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ybd]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_adunca Drosophila adunca], [https://en.wikipedia.org/wiki/Drosophila_saltans Drosophila saltans] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YBD 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=5ybd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ybd OCA], [http://pdbe.org/5ybd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ybd RCSB], [http://www.ebi.ac.uk/pdbsum/5ybd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ybd 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]] 2.769&#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=5ybd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ybd OCA], [https://pdbe.org/5ybd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ybd RCSB], [https://www.ebi.ac.uk/pdbsum/5ybd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ybd ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/ERG_HUMAN ERG_HUMAN]] Defects in ERG are a cause of Ewing sarcoma (ES) [MIM:[http://omim.org/entry/612219 612219]]. A highly malignant, metastatic, primitive small round cell tumor of bone and soft tissue that affects children and adolescents. It belongs to the Ewing sarcoma family of tumors, a group of morphologically heterogeneous neoplasms that share the same cytogenetic features. They are considered neural tumors derived from cells of the neural crest. Ewing sarcoma represents the less differentiated form of the tumors. Note=A chromosomal aberration involving ERG is found in patients with Erwing sarcoma. Translocation t(21;22)(q22;q12) with EWSR1. Note=Chromosomal aberrations involving ERG have been found in acute myeloid leukemia (AML). Translocation t(16;21)(p11;q22) with FUS. Translocation t(X;21)(q25-26;q22) with ELF4.
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[https://www.uniprot.org/uniprot/ERG_HUMAN ERG_HUMAN] Defects in ERG are a cause of Ewing sarcoma (ES) [MIM:[https://omim.org/entry/612219 612219]. A highly malignant, metastatic, primitive small round cell tumor of bone and soft tissue that affects children and adolescents. It belongs to the Ewing sarcoma family of tumors, a group of morphologically heterogeneous neoplasms that share the same cytogenetic features. They are considered neural tumors derived from cells of the neural crest. Ewing sarcoma represents the less differentiated form of the tumors. Note=A chromosomal aberration involving ERG is found in patients with Erwing sarcoma. Translocation t(21;22)(q22;q12) with EWSR1. Note=Chromosomal aberrations involving ERG have been found in acute myeloid leukemia (AML). Translocation t(16;21)(p11;q22) with FUS. Translocation t(X;21)(q25-26;q22) with ELF4.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ERG_HUMAN ERG_HUMAN]] Transcriptional regulator. May participate in transcriptional regulation through the recruitment of SETDB1 histone methyltransferase and subsequent modification of local chromatin structure.
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[https://www.uniprot.org/uniprot/ERG_HUMAN ERG_HUMAN] Transcriptional regulator. May participate in transcriptional regulation through the recruitment of SETDB1 histone methyltransferase and subsequent modification of local chromatin structure.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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ERG3 (ETS-related gene) is a member of the ETS (erythroblast transformation-specific) family of transcription factors, which contain a highly conserved DNA-binding domain. The ETS family of transcription factors differ in their binding to promoter DNA sequences, and the mechanism of their DNA-sequence discrimination is little known. In the current study, crystals of the ETSi domain (the ETS domain of ERG3 containing a CID motif) in space group P41212 and of its complex with the E74 DNA sequence (DNA9) in space group C2221 were obtained and their structures were determined. Comparative structure analysis of the ETSi domain and its complex with DNA9 with previously determined structures of the ERGi domain (the ETS domain of ERG containing inhibitory motifs) in space group P65212 and of the ERGi-DNA12 complex in space group P41212 were performed. The ETSi domain is observed as a homodimer in solution as well as in the crystallographic asymmetric unit. Superposition of the structure of the ETSi domain on that of the ERGi domain showed a major conformational change at the C-terminal DNA-binding autoinhibitory (CID) motif, while minor changes are observed in the loop regions of the ETSi-domain structure. The ETSi-DNA9 complex in space group C2221 forms a structure that is quite similar to that of the ERG-DNA12 complex in space group P41212. Upon superposition of the complexes, major conformational changes are observed at the 5' and 3' ends of DNA9, while the conformation of the core GGA nucleotides was quite conserved. Comparison of the ETSi-DNA9 structure with known structures of ETS class 1 protein-DNA complexes shows the similarities and differences in the promoter DNA binding and specificity of the class 1 ETS proteins.
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Comparative structure analysis of the ETSi domain of ERG3 and its complex with the E74 promoter DNA sequence.,Sharma R, Gangwar SP, Saxena AK Acta Crystallogr F Struct Biol Commun. 2018 Oct 1;74(Pt 10):656-663. doi:, 10.1107/S2053230X1801110X. Epub 2018 Sep 21. PMID:30279318<ref>PMID:30279318</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 5ybd" 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: Gangwar, S P]]
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[[Category: Drosophila adunca]]
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[[Category: Saxena, A K]]
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[[Category: Drosophila saltans]]
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[[Category: Dna binding protein]]
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[[Category: Homo sapiens]]
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[[Category: Dna binding protein-dna complex]]
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[[Category: Large Structures]]
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[[Category: Ets transcription factor]]
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[[Category: Gangwar SP]]
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[[Category: Ets-e74dna complex]]
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[[Category: Saxena AK]]
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[[Category: Human ergp55]]
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Current revision

X-ray structure of ETS domain of Ergp55 in complex with E74DNA

PDB ID 5ybd

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