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5x0y

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Revision as of 22:30, 10 April 2020

Complex of Snf2-Nucleosome complex with Snf2 bound to SHL2 of the nucleosome

5x0y, resolution 4.69Å

Structural highlights

5x0y is a 11 chain structure with sequence from African clawed frog and Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	5x0x
Gene:	hist1h2aj, LOC494591 (African clawed frog), SNF2, GAM1, RIC1, SWI2, TYE3, YOR290C (Baker's yeast)
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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. [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. [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. [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.

Publication Abstract from PubMed

Chromatin remodellers are helicase-like, ATP-dependent enzymes that alter chromatin structure and nucleosome positions to allow regulatory proteins access to DNA. Here we report the cryo-electron microscopy structure of chromatin remodeller Switch/sucrose non-fermentable (SWI2/SNF2) from Saccharomyces cerevisiae bound to the nucleosome. The structure shows that the two core domains of Snf2 are realigned upon nucleosome binding, suggesting activation of the enzyme. The core domains contact each other through two induced Brace helices, which are crucial for coupling ATP hydrolysis to chromatin remodelling. Snf2 binds to the phosphate backbones of one DNA gyre of the nucleosome mainly through its helicase motifs within the major domain cleft, suggesting a conserved mechanism of substrate engagement across different remodellers. Snf2 contacts the second DNA gyre via a positively charged surface, providing a mechanism to anchor the remodeller at a fixed position of the nucleosome. Snf2 locally deforms nucleosomal DNA at the site of binding, priming the substrate for the remodelling reaction. Together, these findings provide mechanistic insights into chromatin remodelling.

Mechanism of chromatin remodelling revealed by the Snf2-nucleosome structure.,Liu X, Li M, Xia X, Li X, Chen Z Nature. 2017 Apr 27;544(7651):440-445. doi: 10.1038/nature22036. Epub 2017 Apr, 19. PMID:28424519^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Liu X, Li M, Xia X, Li X, Chen Z. Mechanism of chromatin remodelling revealed by the Snf2-nucleosome structure. Nature. 2017 Apr 27;544(7651):440-445. doi: 10.1038/nature22036. Epub 2017 Apr, 19. PMID:28424519 doi:http://dx.doi.org/10.1038/nature22036

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5x0y"

@@ Line 3: / Line 3: @@
 <SX load='5x0y' size='340' side='right' viewer='molstar' caption='[[5x0y]], [[Resolution|resolution]] 4.69&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5x0y]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog] and [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X0Y FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5x0y]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog] and [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X0Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5X0Y FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x0x|5x0x]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hist1h2aj, LOC494591 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), SNF2, GAM1, RIC1, SWI2, TYE3, YOR290C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=5x0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x0y OCA], [http://pdbe.org/5x0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x0y RCSB], [http://www.ebi.ac.uk/pdbsum/5x0y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x0y ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5x0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x0y OCA], [http://pdbe.org/5x0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x0y RCSB], [http://www.ebi.ac.uk/pdbsum/5x0y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x0y ProSAT]</span></td></tr>
 </table>
 == Function ==

5x0y

From Proteopedia

Revision as of 22:30, 10 April 2020

Complex of Snf2-Nucleosome complex with Snf2 bound to SHL2 of the nucleosome

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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