6r1t
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of LSD2/NPAC-linker/nucleosome core particle complex: Class 1, free nuclesome== | |
| + | <StructureSection load='6r1t' size='340' side='right'caption='[[6r1t]], [[Resolution|resolution]] 3.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6r1t]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R1T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R1T FirstGlance]. <br> | ||
| + | </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=6r1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r1t OCA], [http://pdbe.org/6r1t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r1t RCSB], [http://www.ebi.ac.uk/pdbsum/6r1t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r1t ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | LSD1 and LSD2 are homologous histone demethylases with opposite biological outcomes related to chromatin silencing and transcription elongation, respectively. Unlike LSD1, LSD2 nucleosome-demethylase activity relies on a specific linker peptide from the multidomain protein NPAC. We used single-particle cryoelectron microscopy (cryo-EM), in combination with kinetic and mutational analysis, to analyze the mechanisms underlying the function of the human LSD2/NPAC-linker/nucleosome complex. Weak interactions between LSD2 and DNA enable multiple binding modes for the association of the demethylase to the nucleosome. The demethylase thereby captures mono- and dimethyl Lys4 of the H3 tail to afford histone demethylation. Our studies also establish that the dehydrogenase domain of NPAC serves as a catalytically inert oligomerization module. While LSD1/CoREST forms a nucleosome docking platform at silenced gene promoters, LSD2/NPAC is a multifunctional enzyme complex with flexible linkers, tailored for rapid chromatin modification, in conjunction with the advance of the RNA polymerase on actively transcribed genes. | ||
| - | + | A Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex.,Marabelli C, Marrocco B, Pilotto S, Chittori S, Picaud S, Marchese S, Ciossani G, Forneris F, Filippakopoulos P, Schoehn G, Rhodes D, Subramaniam S, Mattevi A Cell Rep. 2019 Apr 9;27(2):387-399.e7. doi: 10.1016/j.celrep.2019.03.061. PMID:30970244<ref>PMID:30970244</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6r1t" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chittori, S]] | ||
| + | [[Category: Marabelli, C]] | ||
| + | [[Category: Mattevi, A]] | ||
| + | [[Category: Pilotto, S]] | ||
| + | [[Category: Subramaniam, S]] | ||
| + | [[Category: Chromatin reader]] | ||
| + | [[Category: Epigenetic]] | ||
| + | [[Category: Evolution of protein function]] | ||
| + | [[Category: Flavoenzyme]] | ||
| + | [[Category: Gene regulation]] | ||
| + | [[Category: Histone demethylation]] | ||
| + | [[Category: Molecular recognition]] | ||
Revision as of 07:13, 24 April 2019
Structure of LSD2/NPAC-linker/nucleosome core particle complex: Class 1, free nuclesome
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