4EO5

Yeast Asf1 bound to H3/H4G94P mutant

Summary for 4EO5

• Entry DOI: 10.2210/pdb4eo5/pdb
• Descriptor: Histone chaperone ASF1, Histone H3.2, Histone H4, ... (6 entities in total)
• Functional Keywords: ig-like domain, histone fold, nucleosome assembly, histone chaperone, structural protein-chaperone complex, structural protein/chaperone
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus: P32447 P84233 P62799
• Total number of polymer chains: 3
• Total formula weight: 37514.92

Authors

Scorgie, J.K.,Churchill, M.E. (deposition date: 2012-04-13, release date: 2012-06-13, Last modification date: 2023-09-13)

Primary citation

Chavez, M.S.,Scorgie, J.K.,Dennehey, B.K.,Noone, S.M.,Tyler, J.K.,Churchill, M.E.
The conformational flexibility of the C-terminus of histone H4 promotes histone octamer and nucleosome stability and yeast viability.
Epigenetics Chromatin, 5:5-5, 2012

PubMed Abstract: The protein anti-silencing function 1 (Asf1) chaperones histones H3/H4 for assembly into nucleosomes every cell cycle as well as during DNA transcription and repair. Asf1 interacts directly with H4 through the C-terminal tail of H4, which itself interacts with the docking domain of H2A in the nucleosome. The structure of this region of the H4 C-terminus differs greatly in these two contexts.

PubMed: 22541333
DOI: 10.1186/1756-8935-5-5

Experimental method

X-RAY DIFFRACTION (2.35 Å)