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5z3v

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==Structure of Snf2-nucleosome complex at shl-2 in ADP BeFx state==
==Structure of Snf2-nucleosome complex at shl-2 in ADP BeFx state==
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<StructureSection load='5z3v' size='340' side='right'caption='[[5z3v]], [[Resolution|resolution]] 4.22&Aring;' scene=''>
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<SX load='5z3v' size='340' side='right' viewer='molstar' caption='[[5z3v]], [[Resolution|resolution]] 4.22&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5z3v]] is a 11 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z3V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z3V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5z3v]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C], [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z3V FirstGlance]. <br>
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</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>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.22&#8491;</td></tr>
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<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=5z3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z3v OCA], [http://pdbe.org/5z3v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z3v RCSB], [http://www.ebi.ac.uk/pdbsum/5z3v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z3v ProSAT]</span></td></tr>
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<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>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5z3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z3v OCA], [https://pdbe.org/5z3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5z3v RCSB], [https://www.ebi.ac.uk/pdbsum/5z3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5z3v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SNF2_YEAST SNF2_YEAST]] Involved in transcriptional activation. Catalytic component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. [[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/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. [[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.
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Chromatin remodellers include diverse enzymes with distinct biological functions, but nucleosome-sliding activity appears to be a common theme(1,2). Among the remodelling enzymes, Snf2 serves as the prototype to study the action of this protein family. Snf2 and related enzymes share two conserved RecA-like lobes(3), which by themselves are able to couple ATP hydrolysis to chromatin remodelling. The mechanism by which these enzymes couple ATP hydrolysis to translocate the nucleosome along the DNA remains unclear(2,4-8). Here we report the structures of Saccharomyces cerevisiae Snf2 bound to the nucleosome in the presence of ADP and ADP-BeFx. Snf2 in the ADP-bound state adopts an open conformation similar to that in the apo state, and induces a one-base-pair DNA bulge at superhelix location 2 (SHL2), with the tracking strand showing greater distortion than the guide strand. The DNA distortion propagates to the proximal end, leading to staggered translocation of the two strands. The binding of ADP-BeFx triggers a closed conformation of the enzyme, resetting the nucleosome to a relaxed state. Snf2 shows altered interactions with the DNA in different nucleotide states, providing the structural basis for DNA translocation. Together, our findings suggest a fundamental mechanism for the DNA translocation that underlies chromatin remodelling.
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Mechanism of DNA translocation underlying chromatin remodelling by Snf2.,Li M, Xia X, Tian Y, Jia Q, Liu X, Lu Y, Li M, Li X, Chen Z Nature. 2019 Mar;567(7748):409-413. doi: 10.1038/s41586-019-1029-2. Epub 2019 Mar, 13. PMID:30867599<ref>PMID:30867599</ref>
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==See Also==
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*[[Helicase 3D structures|Helicase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[Histone 3D structures|Histone 3D structures]]
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</div>
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<div class="pdbe-citations 5z3v" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
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</StructureSection>
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</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, Z]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Li, M]]
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[[Category: Synthetic construct]]
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[[Category: Li, X]]
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[[Category: Xenopus laevis]]
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[[Category: Liu, X]]
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[[Category: Chen Z]]
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[[Category: Xia, X]]
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[[Category: Li M]]
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[[Category: Chromatin remodeling]]
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[[Category: Li X]]
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[[Category: Complex]]
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[[Category: Liu X]]
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[[Category: Gene regulation]]
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[[Category: Xia X]]
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[[Category: Nucleosome]]
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[[Category: Structural protein-hydrolase-dna complex]]
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Current revision

Structure of Snf2-nucleosome complex at shl-2 in ADP BeFx state

5z3v, resolution 4.22Å

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