6ww4
From Proteopedia
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==Crystal structure of HERC2 ZZ domain in complex with histone H3 tail== | ==Crystal structure of HERC2 ZZ domain in complex with histone H3 tail== | ||
| - | <StructureSection load='6ww4' size='340' side='right'caption='[[6ww4]]' scene=''> | + | <StructureSection load='6ww4' size='340' side='right'caption='[[6ww4]], [[Resolution|resolution]] 2.25Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WW4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WW4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ww4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WW4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WW4 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ww4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ww4 OCA], [http://pdbe.org/6ww4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ww4 RCSB], [http://www.ebi.ac.uk/pdbsum/6ww4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ww4 ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HERC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.26 2.3.2.26] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ww4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ww4 OCA], [http://pdbe.org/6ww4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ww4 RCSB], [http://www.ebi.ac.uk/pdbsum/6ww4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ww4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Human ubiquitin ligase HERC2, a component of the DNA repair machinery, has been linked to neurological diseases and cancer. Here, we show that the ZZ domain of HERC2 (HERC2ZZ) binds to histone H3 tail and tolerates posttranslational modifications commonly present in H3. The crystal structure of the HERC2ZZ:H3 complex provides the molecular basis for this interaction and highlights a critical role of the negatively charged site of HERC2ZZ in capturing of A1 of H3. NMR, mutagenesis, and fluorescence data reveal that HERC2ZZ binds to H3 and the N-terminal tail of SUMO1, a previously reported ligand of HERC2ZZ, with comparable affinities. Like H3, the N-terminal tail of SUMO1 occupies the same negatively charged site of HERC2ZZ in the crystal structure of the complex, although in contrast to H3 it adopts an alpha-helical conformation. Our data suggest that HERC2ZZ may play a role in mediating the association of HERC2 with chromatin. | ||
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| + | Structural Insight into Binding of the ZZ Domain of HERC2 to Histone H3 and SUMO1.,Liu J, Xue Z, Zhang Y, Vann KR, Shi X, Kutateladze TG Structure. 2020 Jul 23. pii: S0969-2126(20)30236-7. doi:, 10.1016/j.str.2020.07.003. PMID:32726574<ref>PMID:32726574</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6ww4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Kutateladze | + | [[Category: Transferase]] |
| - | [[Category: Liu J]] | + | [[Category: Kutateladze, T G]] |
| - | [[Category: Vann | + | [[Category: Liu, J]] |
| + | [[Category: Vann, K R]] | ||
| + | [[Category: Gene regulation]] | ||
| + | [[Category: Herc2]] | ||
| + | [[Category: Histone reader]] | ||
| + | [[Category: Zinc finger protein]] | ||
| + | [[Category: Zz domain]] | ||
Revision as of 10:05, 12 August 2020
Crystal structure of HERC2 ZZ domain in complex with histone H3 tail
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