4khb: Difference between revisions
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==Structure of the Spt16D Pob3N heterodimer== | ==Structure of the Spt16D Pob3N heterodimer== | ||
<StructureSection load='4khb' size='340' side='right' caption='[[4khb]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='4khb' size='340' side='right'caption='[[4khb]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4khb]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4khb]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KHB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KHB FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4khb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4khb OCA], [https://pdbe.org/4khb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4khb RCSB], [https://www.ebi.ac.uk/pdbsum/4khb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4khb ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/G0SDN1_CHATD G0SDN1_CHATD] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Ladurner AG]] | ||
[[Category: | [[Category: Stuwe T]] | ||
[[Category: | [[Category: Zhang E]] | ||
Revision as of 14:58, 30 November 2022
Structure of the Spt16D Pob3N heterodimerStructure of the Spt16D Pob3N heterodimer
Structural highlights
FunctionPublication Abstract from PubMedFacilitates chromatin transcription (FACT) is a conserved histone chaperone that reorganizes nucleosomes and ensures chromatin integrity during DNA transcription, replication and repair. Key to the broad functions of FACT is its recognition of histones H2A-H2B (ref. 2). However, the structural basis for how histones H2A-H2B are recognized and how this integrates with the other functions of FACT, including the recognition of histones H3-H4 and other nuclear factors, is unknown. Here we reveal the crystal structure of the evolutionarily conserved FACT chaperone domain Spt16M from Chaetomium thermophilum, in complex with the H2A-H2B heterodimer. A novel 'U-turn' motif scaffolded onto a Rtt106-like module embraces the alpha1 helix of H2B. Biochemical and in vivo assays validate the structure and dissect the contribution of histone tails and H3-H4 towards Spt16M binding. Furthermore, we report the structure of the FACT heterodimerization domain that connects FACT to replicative polymerases. Our results show that Spt16M makes several interactions with histones, which we suggest allow the module to invade the nucleosome gradually and block the strongest interaction of H2B with DNA. FACT would thus enhance 'nucleosome breathing' by re-organizing the first 30 base pairs of nucleosomal histone-DNA contacts. Our snapshot of the engagement of the chaperone with H2A-H2B and the structures of all globular FACT domains enable the high-resolution analysis of the vital chaperoning functions of FACT, shedding light on how the complex promotes the activity of enzymes that require nucleosome reorganization. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT.,Hondele M, Stuwe T, Hassler M, Halbach F, Bowman A, Zhang ET, Nijmeijer B, Kotthoff C, Rybin V, Amlacher S, Hurt E, Ladurner AG Nature. 2013 May 22. doi: 10.1038/nature12242. PMID:23698368[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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