6ne3
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of singly-bound SNF2h-nucleosome complex with SNF2h bound at SHL-2== | |
| + | <StructureSection load='6ne3' size='340' side='right'caption='[[6ne3]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ne3]] is a 11 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NE3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NE3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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=6ne3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ne3 OCA], [http://pdbe.org/6ne3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ne3 RCSB], [http://www.ebi.ac.uk/pdbsum/6ne3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ne3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/SMCA5_HUMAN SMCA5_HUMAN]] Extraskeletal Ewing sarcoma. | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/H2A1_XENLA H2A1_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/H4_XENLA H4_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/SMCA5_HUMAN SMCA5_HUMAN]] Helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity. Complexes containing SMARCA5 are capable of forming ordered nucleosome arrays on chromatin; this may require intact histone H4 tails. Also required for replication of pericentric heterochromatin in S-phase specifically in conjunction with BAZ1A. Probably plays a role in repression of polI dependent transcription of the rDNA locus, through the recruitment of the SIN3/HDAC1 corepressor complex to the rDNA promoter. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing.<ref>PMID:10880450</ref> <ref>PMID:11980720</ref> <ref>PMID:12198550</ref> <ref>PMID:12434153</ref> <ref>PMID:12972596</ref> <ref>PMID:15543136</ref> <ref>PMID:16603771</ref> [[http://www.uniprot.org/uniprot/H32_XENLA H32_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The SNF2h remodeler slides nucleosomes most efficiently as a dimer, yet how the two protomers avoid a tug-of-war is unclear. Furthermore, SNF2h couples histone octamer deformation to nucleosome sliding, but the underlying structural basis remains unknown. Here we present cryo-EM structures of SNF2h-nucleosome complexes with ADP-BeFx that capture two potential reaction intermediates. In one structure, histone residues near the dyad and in the H2A-H2B acidic patch, distal to the active SNF2h protomer, appear disordered. The disordered acidic patch is expected to inhibit the second SNF2h protomer, while disorder near the dyad is expected to promote DNA translocation. The other structure doesn't show octamer deformation, but surprisingly shows a 2 bp translocation. FRET studies indicate that ADP-BeFx predisposes SNF2h-nucleosome complexes for an elemental translocation step. We propose a model for allosteric control through the nucleosome, where one SNF2h protomer promotes asymmetric octamer deformation to inhibit the second protomer, while stimulating directional DNA translocation. | ||
| - | + | Cryo-EM structures of remodeler-nucleosome intermediates suggest allosteric control through the nucleosome.,Armache JP, Gamarra N, Johnson SL, Leonard JD, Wu S, Narlikar GJ, Cheng Y Elife. 2019 Jun 18;8. pii: 46057. doi: 10.7554/eLife.46057. PMID:31210637<ref>PMID:31210637</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6ne3" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Armache, J P]] | ||
| + | [[Category: Cheng, Y]] | ||
| + | [[Category: Gamarra, N]] | ||
| + | [[Category: Johnson, S L]] | ||
| + | [[Category: Leonard, J D]] | ||
| + | [[Category: Narlikar, G N]] | ||
| + | [[Category: Wu, S]] | ||
| + | [[Category: Chromatin]] | ||
| + | [[Category: Dna]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: Dna binding protein-dna complex]] | ||
| + | [[Category: Histone]] | ||
| + | [[Category: Iswi]] | ||
| + | [[Category: Nucleosome]] | ||
| + | [[Category: Snf2h]] | ||
Revision as of 10:47, 17 July 2019
Cryo-EM structure of singly-bound SNF2h-nucleosome complex with SNF2h bound at SHL-2
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Categories: Large Structures | Armache, J P | Cheng, Y | Gamarra, N | Johnson, S L | Leonard, J D | Narlikar, G N | Wu, S | Chromatin | Dna | Dna binding protein | Dna binding protein-dna complex | Histone | Iswi | Nucleosome | Snf2h
