6min: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of Taf14 YEATS domain G82A mutant in complex with histone H3K9cr== | ==Crystal structure of Taf14 YEATS domain G82A mutant in complex with histone H3K9cr== | ||
<StructureSection load='6min' size='340' side='right' caption='[[6min]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='6min' size='340' side='right'caption='[[6min]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6min]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MIN OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6min]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MIN FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=KCR:N-6-CROTONYL-L-LYSINE'>KCR</scene></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=6min FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6min OCA], [https://pdbe.org/6min PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6min RCSB], [https://www.ebi.ac.uk/pdbsum/6min PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6min ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/H31_HUMAN H31_HUMAN] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 6min" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6min" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Histone 3D structures|Histone 3D structures]] | |||
*[[Transcription initiation factors 3D structures|Transcription initiation factors 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae S288C]] | ||
[[Category: | [[Category: Andrews FH]] | ||
[[Category: | [[Category: Klein BJ]] | ||
[[Category: | [[Category: Kutateladze TG]] | ||
Latest revision as of 09:32, 11 October 2023
Crystal structure of Taf14 YEATS domain G82A mutant in complex with histone H3K9crCrystal structure of Taf14 YEATS domain G82A mutant in complex with histone H3K9cr
Structural highlights
FunctionPublication Abstract from PubMedThe YEATS domain has been identified as a reader of histone acylation and more recently emerged as a promising anti-cancer therapeutic target. Here, we detail the structural mechanisms for pi-pi-pi stacking involving the YEATS domains of yeast Taf14 and human AF9 and acylated histone H3 peptides and explore DNA-binding activities of these domains. Taf14-YEATS selects for crotonyllysine, forming pi stacking with both the crotonyl amide and the alkene moiety, whereas AF9-YEATS exhibits comparable affinities to saturated and unsaturated acyllysines, engaging them through pi stacking with the acyl amide. Importantly, AF9-YEATS is capable of binding to DNA, whereas Taf14-YEATS is not. Using a structure-guided approach, we engineered a mutant of Taf14-YEATS that engages crotonyllysine through the aromatic-aliphatic-aromatic pi stacking and shows high selectivity for the crotonyl H3K9 modification. Our findings shed light on the molecular principles underlying recognition of acyllysine marks and reveal a previously unidentified DNA-binding activity of AF9-YEATS. Structural insights into the pi-pi-pi stacking mechanism and DNA-binding activity of the YEATS domain.,Klein BJ, Vann KR, Andrews FH, Wang WW, Zhang J, Zhang Y, Beloglazkina AA, Mi W, Li Y, Li H, Shi X, Kutateladze AG, Strahl BD, Liu WR, Kutateladze TG Nat Commun. 2018 Nov 1;9(1):4574. doi: 10.1038/s41467-018-07072-6. PMID:30385749[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||