8ia3: Difference between revisions
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==Crystal structure of human USF2 bHLHLZ domain in complex with DNA== | |||
<StructureSection load='8ia3' size='340' side='right'caption='[[8ia3]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8ia3]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IA3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IA3 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ia3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ia3 OCA], [https://pdbe.org/8ia3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ia3 RCSB], [https://www.ebi.ac.uk/pdbsum/8ia3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ia3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/USF2_HUMAN USF2_HUMAN] Transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Upstream stimulating factors (USFs), including USF1 and USF2, are key components of the transcription machinery that recruit coactivators and histone-modifying enzymes. Using the classic basic Helix-Loop-Helix Leucine Zipper (bHLH-LZ) domain, USFs bind the E-box DNA and form tetramers that promote DNA looping for transcription initiation. The structural basis by which USFs tetramerize and to bind DNA , however, remains unknown. Here, we report the crystal structure of the complete bHLH-LZ domain of USF2 in complex with E-box DNA. We observed that the LZ of USF2 is longer than that of other bHLH-LZ family transcription factors and that the C-terminus of USF2 forms an additional alpha-helix following the LZ region (denoted as LZ-Ext). We also found the elongated LZ-Ext facilitates compact tetramer formation. In addition to the classic interactions between the basic region and DNA, we show a highly conserved basic residue in the loop region, Lys271, participates in DNA interaction. Together, these findings suggest that USF2 forms a tetramer structure with a bent elongated LZ-Ext region, providing a molecular basis for its role as a key component of the transcription machinery. | |||
Tetramerization of upstream stimulating factor USF2 requires the elongated bent leucine zipper of the bHLH-LZ domain.,Huang C, Xia M, Qiao H, Liu Z, Lin Y, Sun H, Yu B, Fang P, Wang J J Biol Chem. 2023 Sep 8:105240. doi: 10.1016/j.jbc.2023.105240. PMID:37690682<ref>PMID:37690682</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8ia3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Fang P]] | |||
[[Category: Huang C]] | |||
[[Category: Wang J]] | |||
Latest revision as of 17:44, 20 September 2023
Crystal structure of human USF2 bHLHLZ domain in complex with DNACrystal structure of human USF2 bHLHLZ domain in complex with DNA
Structural highlights
FunctionUSF2_HUMAN Transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters. Publication Abstract from PubMedUpstream stimulating factors (USFs), including USF1 and USF2, are key components of the transcription machinery that recruit coactivators and histone-modifying enzymes. Using the classic basic Helix-Loop-Helix Leucine Zipper (bHLH-LZ) domain, USFs bind the E-box DNA and form tetramers that promote DNA looping for transcription initiation. The structural basis by which USFs tetramerize and to bind DNA , however, remains unknown. Here, we report the crystal structure of the complete bHLH-LZ domain of USF2 in complex with E-box DNA. We observed that the LZ of USF2 is longer than that of other bHLH-LZ family transcription factors and that the C-terminus of USF2 forms an additional alpha-helix following the LZ region (denoted as LZ-Ext). We also found the elongated LZ-Ext facilitates compact tetramer formation. In addition to the classic interactions between the basic region and DNA, we show a highly conserved basic residue in the loop region, Lys271, participates in DNA interaction. Together, these findings suggest that USF2 forms a tetramer structure with a bent elongated LZ-Ext region, providing a molecular basis for its role as a key component of the transcription machinery. Tetramerization of upstream stimulating factor USF2 requires the elongated bent leucine zipper of the bHLH-LZ domain.,Huang C, Xia M, Qiao H, Liu Z, Lin Y, Sun H, Yu B, Fang P, Wang J J Biol Chem. 2023 Sep 8:105240. doi: 10.1016/j.jbc.2023.105240. PMID:37690682[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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