4ld9: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(4 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{STRUCTURE_4ld9|  PDB=4ld9  |  SCENE=  }}
===Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle===


==Function==
==Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle==
[[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. [[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/SIR3_YEAST SIR3_YEAST]] The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form. [[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.  
<StructureSection load='4ld9' size='340' side='right'caption='[[4ld9]], [[Resolution|resolution]] 3.31&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ld9]] is a 12 chain structure with sequence from [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=4LD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LD9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.306&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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=4ld9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ld9 OCA], [https://pdbe.org/4ld9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ld9 RCSB], [https://www.ebi.ac.uk/pdbsum/4ld9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ld9 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The N-terminal acetylation of Sir3 is essential for heterochromatin establishment and maintenance in yeast, but its mechanism of action is unknown. The crystal structure of the N-terminally acetylated BAH domain of Saccharomyces cerevisiae Sir3 bound to the nucleosome core particle reveals that the N-terminal acetylation stabilizes the interaction of Sir3 with the nucleosome. Additionally, we present a new method for the production of protein-nucleosome complexes for structural analysis.


==About this Structure==
The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle.,Arnaudo N, Fernandez IS, McLaughlin SH, Peak-Chew SY, Rhodes D, Martino F Nat Struct Mol Biol. 2013 Aug 11. doi: 10.1038/nsmb.2641. PMID:23934150<ref>PMID:23934150</ref>
[[4ld9]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LD9 OCA].
 
[[Category: Saccharomyces cerevisiae s288c]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ld9" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Histone 3D structures|Histone 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
[[Category: Arnaudo, N.]]
[[Category: Arnaudo N]]
[[Category: Fernandez, I S.]]
[[Category: Fernandez IS]]
[[Category: Martino, F.]]
[[Category: Martino F]]
[[Category: McLaughlin, S H.]]
[[Category: McLaughlin SH]]
[[Category: Peak-Chew, S Y.]]
[[Category: Peak-Chew SY]]
[[Category: Rhodes, D.]]
[[Category: Rhodes D]]
[[Category: Alpha-helix]]
[[Category: Beta barrel]]
[[Category: Beta-sheet]]
[[Category: Chromatin]]
[[Category: Chromatin binding]]
[[Category: Double helix]]
[[Category: Double stranded dna]]
[[Category: N-terminal acetylation]]
[[Category: Nuclear protein-transcription-dna complex]]
[[Category: Nucleus]]
[[Category: Protein-dna complex]]

Latest revision as of 06:11, 21 November 2024

Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particleCrystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle

Structural highlights

4ld9 is a 12 chain structure with sequence from Saccharomyces cerevisiae S288C and Xenopus laevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.306Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

The N-terminal acetylation of Sir3 is essential for heterochromatin establishment and maintenance in yeast, but its mechanism of action is unknown. The crystal structure of the N-terminally acetylated BAH domain of Saccharomyces cerevisiae Sir3 bound to the nucleosome core particle reveals that the N-terminal acetylation stabilizes the interaction of Sir3 with the nucleosome. Additionally, we present a new method for the production of protein-nucleosome complexes for structural analysis.

The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle.,Arnaudo N, Fernandez IS, McLaughlin SH, Peak-Chew SY, Rhodes D, Martino F Nat Struct Mol Biol. 2013 Aug 11. doi: 10.1038/nsmb.2641. PMID:23934150[1]

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

See Also

References

  1. ↑ Arnaudo N, Fernandez IS, McLaughlin SH, Peak-Chew SY, Rhodes D, Martino F. The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle. Nat Struct Mol Biol. 2013 Aug 11. doi: 10.1038/nsmb.2641. PMID:23934150 doi:10.1038/nsmb.2641

4ld9, resolution 3.31Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=4ld9&oldid=4216237"