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| ==the crosslinked complex of ISWI-nucleosome in the ADP-bound state== | | ==the crosslinked complex of ISWI-nucleosome in the ADP-bound state== |
| <StructureSection load='6iro' size='340' side='right'caption='[[6iro]], [[Resolution|resolution]] 3.40Å' scene=''> | | <SX load='6iro' size='340' side='right' viewer='molstar' caption='[[6iro]], [[Resolution|resolution]] 3.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6iro]] is a 11 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IRO FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6iro]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12], [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IRO 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> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</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=6iro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iro OCA], [http://pdbe.org/6iro PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iro RCSB], [http://www.ebi.ac.uk/pdbsum/6iro PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iro ProSAT]</span></td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=6iro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iro OCA], [https://pdbe.org/6iro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iro RCSB], [https://www.ebi.ac.uk/pdbsum/6iro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iro ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/ISW1_YEAST ISW1_YEAST]] Catalytic component of ISW1-type complexes, which act by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. They are involved in coordinating transcriptional repression, activation and elongation phases. The ISW1A complex represses gene expression at initiation through specific positioning of a promoter proximal dinucleosome. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing.<ref>PMID:10090725</ref> <ref>PMID:11238381</ref> <ref>PMID:14622597</ref> <ref>PMID:12482963</ref> [[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/H2B11_XENLA H2B11_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. | | [https://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. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Chromatin remodelers are diverse enzymes, and different models have been proposed to explain how these proteins work. Here we report the 3.3 A-resolution cryogenic electron microscopy (cryo-EM) structures of Saccharomyces cerevisiae ISWI (ISW1) in complex with the nucleosome in adenosine diphosphate (ADP)-bound and ADP-BeFx-bound states. The data show that after nucleosome binding, ISW1 is activated by substantial rearrangement of the catalytic domains, with the regulatory AutoN domain packing the first RecA-like core and the NegC domain being disordered. The high-resolution structure reveals local DNA distortion and translocation induced by ISW1 in the ADP-bound state, which is essentially identical to that induced by the Snf2 chromatin remodeler, suggesting a common mechanism of DNA translocation. The histone core remains largely unperturbed, and prevention of histone distortion by crosslinking did not inhibit the activity of yeast ISW1 or its human homolog. Together, our findings suggest a general mechanism of chromatin remodeling involving local DNA distortion without notable histone deformation.
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| Structures of the ISWI-nucleosome complex reveal a conserved mechanism of chromatin remodeling.,Yan L, Wu H, Li X, Gao N, Chen Z Nat Struct Mol Biol. 2019 Mar 13. pii: 10.1038/s41594-019-0199-9. doi:, 10.1038/s41594-019-0199-9. PMID:30872815<ref>PMID:30872815</ref>
| | ==See Also== |
| | | *[[Histone 3D structures|Histone 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6iro" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </SX> |
| | [[Category: Escherichia coli K-12]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Chen, Z C]] | | [[Category: Saccharomyces cerevisiae S288C]] |
| [[Category: Gao, N]] | | [[Category: Xenopus laevis]] |
| [[Category: Li, X M]] | | [[Category: Chen ZC]] |
| [[Category: Wu, H]] | | [[Category: Gao N]] |
| [[Category: Yan, L J]] | | [[Category: Li XM]] |
| [[Category: Chromatin remodelling]] | | [[Category: Wu H]] |
| [[Category: Dna binding protein]] | | [[Category: Yan LJ]] |
| [[Category: Dna binding protein-dna complex]]
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| [[Category: Nucleosome]]
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| [[Category: Single particle cryo-em]]
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