4HGA

Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX

Summary for 4HGA

• Entry DOI: 10.2210/pdb4hga/pdb
• Descriptor: Death domain-associated protein 6, Histone H3.3, Histone H4, ... (5 entities in total)
• Functional Keywords: histone chaperone, chaperone-apoptosis complex, chaperone/apoptosis
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q9UER7; Nucleus: P84243 P62805
• Total number of polymer chains: 3
• Total formula weight: 52908.33

Authors

Liu, C.P.,Xiong, C.Y.,Wang, M.Z.,Yu, Z.L.,Yang, N.,Chen, P.,Zhang, Z.G.,Li, G.H.,Xu, R.M. (deposition date: 2012-10-07, release date: 2012-11-07, Last modification date: 2024-03-20)

Primary citation

Liu, C.P.,Xiong, C.Y.,Wang, M.Z.,Yu, Z.L.,Yang, N.,Chen, P.,Zhang, Z.G.,Li, G.H.,Xu, R.M.
Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX.
Nat.Struct.Mol.Biol., 19:1287-1292, 2012

PubMed Abstract: Mammalian histone H3.3 is a variant of the canonical H3.1 essential for genome reprogramming in fertilized eggs and maintenance of chromatin structure in neuronal cells. An H3.3-specific histone chaperone, DAXX, directs the deposition of H3.3 onto pericentric and telomeric heterochromatin. H3.3 differs from H3.1 by only five amino acids, yet DAXX can distinguish the two with high precision. By a combination of structural, biochemical and cell-based targeting analyses, we show that Ala87 and Gly90 are the principal determinants of human H3.3 specificity. DAXX uses a shallow hydrophobic pocket to accommodate the small hydrophobic Ala87 of H3.3, whereas a polar binding environment in DAXX prefers Gly90 in H3.3 over the hydrophobic Met90 in H3.1. An H3.3-H4 heterodimer is bound by the histone-binding domain of DAXX, which makes extensive contacts with both H3.3 and H4.

PubMed: 23142979
DOI: 10.1038/nsmb.2439

Experimental method

X-RAY DIFFRACTION (2.799 Å)