6OM3

Crystal structure of the Orc1 BAH domain in complex with a nucleosome core particle

Summary for 6OM3

• Entry DOI: 10.2210/pdb6om3/pdb
• Descriptor: Histone H3.2, Histone H4, Histone H2A, ... (7 entities in total)
• Functional Keywords: chromatin modifier, structural protein, structural protein-dna complex, structural protein/dna
• Biological source: Xenopus laevis (African clawed frog); More
• Total number of polymer chains: 24
• Total formula weight: 504285.53

Authors

De Ioannes, P.E.,Wang, M.,Armache, K.-J. (deposition date: 2019-04-18, release date: 2019-07-10, Last modification date: 2024-10-23)

Primary citation

De Ioannes, P.,Leon, V.A.,Kuang, Z.,Wang, M.,Boeke, J.D.,Hochwagen, A.,Armache, K.J.
Structure and function of the Orc1 BAH-nucleosome complex.
Nat Commun, 10:2894-2894, 2019

PubMed Abstract: The Origin Recognition Complex (ORC) is essential for replication, heterochromatin formation, telomere maintenance and genome stability in eukaryotes. Here we present the structure of the yeast Orc1 BAH domain bound to the nucleosome core particle. Our data reveal that Orc1, unlike its close homolog Sir3 involved in gene silencing, does not appear to discriminate between acetylated and non-acetylated lysine 16, modification states of the histone H4 tail that specify open and closed chromatin respectively. We elucidate the mechanism for this unique feature of Orc1 and hypothesize that its ability to interact with nucleosomes regardless of K16 modification state enables it to perform critical functions in both hetero- and euchromatin. We also show that direct interactions with nucleosomes are essential for Orc1 to maintain the integrity of rDNA borders during meiosis, a process distinct and independent from its known roles in silencing and replication.

PubMed: 31263106
DOI: 10.1038/s41467-019-10609-y

Experimental method

X-RAY DIFFRACTION (3.3 Å)