5oqd: Difference between revisions
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==PHD2 and winged-helix domain of Polycomblike== | |||
<StructureSection load='5oqd' size='340' side='right' caption='[[5oqd]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5oqd]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OQD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OQD FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5oqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oqd OCA], [http://pdbe.org/5oqd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oqd RCSB], [http://www.ebi.ac.uk/pdbsum/5oqd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oqd ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Polycomb repressive complex 2 (PRC2) trimethylates histone H3 at lysine 27 to mark genes for repression. We measured the dynamics of PRC2 binding on recombinant chromatin and free DNA at the single-molecule level using total internal reflection fluorescence (TIRF) microscopy. PRC2 preferentially binds free DNA with multisecond residence time and midnanomolar affinity. PHF1, a PRC2 accessory protein of the Polycomblike family, extends PRC2 residence time on DNA and chromatin. Crystallographic and functional studies reveal that Polycomblike proteins contain a winged-helix domain that binds DNA in a sequence-nonspecific fashion. DNA binding by this winged-helix domain accounts for the prolonged residence time of PHF1-PRC2 on chromatin and makes it a more efficient H3K27 methyltranferase than PRC2 alone. Together, these studies establish that interactions with DNA provide the predominant binding affinity of PRC2 for chromatin. Moreover, they reveal the molecular basis for how Polycomblike proteins stabilize PRC2 on chromatin and stimulate its activity. | |||
DNA binding by PHF1 prolongs PRC2 residence time on chromatin and thereby promotes H3K27 methylation.,Choi J, Bachmann AL, Tauscher K, Benda C, Fierz B, Muller J Nat Struct Mol Biol. 2017 Oct 23. doi: 10.1038/nsmb.3488. PMID:29058710<ref>PMID:29058710</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5oqd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Benda, C]] | |||
[[Category: Choi, J]] | |||
[[Category: Mueller, J]] | |||
[[Category: Gene regulation]] | |||
[[Category: Phd finger domain]] | |||
[[Category: Polycomblike]] | |||
[[Category: Winged-helix domain]] | |||
Revision as of 09:17, 1 November 2017
PHD2 and winged-helix domain of PolycomblikePHD2 and winged-helix domain of Polycomblike
Structural highlights
Publication Abstract from PubMedPolycomb repressive complex 2 (PRC2) trimethylates histone H3 at lysine 27 to mark genes for repression. We measured the dynamics of PRC2 binding on recombinant chromatin and free DNA at the single-molecule level using total internal reflection fluorescence (TIRF) microscopy. PRC2 preferentially binds free DNA with multisecond residence time and midnanomolar affinity. PHF1, a PRC2 accessory protein of the Polycomblike family, extends PRC2 residence time on DNA and chromatin. Crystallographic and functional studies reveal that Polycomblike proteins contain a winged-helix domain that binds DNA in a sequence-nonspecific fashion. DNA binding by this winged-helix domain accounts for the prolonged residence time of PHF1-PRC2 on chromatin and makes it a more efficient H3K27 methyltranferase than PRC2 alone. Together, these studies establish that interactions with DNA provide the predominant binding affinity of PRC2 for chromatin. Moreover, they reveal the molecular basis for how Polycomblike proteins stabilize PRC2 on chromatin and stimulate its activity. DNA binding by PHF1 prolongs PRC2 residence time on chromatin and thereby promotes H3K27 methylation.,Choi J, Bachmann AL, Tauscher K, Benda C, Fierz B, Muller J Nat Struct Mol Biol. 2017 Oct 23. doi: 10.1038/nsmb.3488. PMID:29058710[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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