4ld9: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4ld9|  PDB=4ld9  |  SCENE=  }}
===Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle===


The entry 4ld9 is ON HOLD  until Paper Publication
==Function==
[[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.


Authors: Arnaudo, N., Fernandez, I.S., McLaughlin, S.H., Peak-Chew, S.Y., Rhodes, D., Martino, F.
==About this Structure==
 
[[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].
Description: Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle
[[Category: Saccharomyces cerevisiae s288c]]
[[Category: Xenopus laevis]]
[[Category: Arnaudo, N.]]
[[Category: Fernandez, I S.]]
[[Category: Martino, F.]]
[[Category: McLaughlin, S H.]]
[[Category: Peak-Chew, S Y.]]
[[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]]