2HUE

Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4

Summary for 2HUE

• Entry DOI: 10.2210/pdb2hue/pdb
• Related: 1KX5 1ROC
• Descriptor: Anti-silencing protein 1, Histone H3, Histone H4, ... (7 entities in total)
• Functional Keywords: mini beta sheet, elongated beta sandwhich, dna binding protein
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Nucleus : P32447 P62799; Chromosome : Q92133
• Total number of polymer chains: 3
• Total formula weight: 38534.41

Authors

English, C.M.,Churchill, M.E.A.,Tyler, J.K. (deposition date: 2006-07-26, release date: 2006-11-21, Last modification date: 2024-02-14)

Primary citation

English, C.M.,Adkins, M.W.,Carson, J.J.,Churchill, M.E.,Tyler, J.K.
Structural basis for the histone chaperone activity of asf1.
Cell(Cambridge,Mass.), 127:495-508, 2006

PubMed Abstract: Anti-silencing function 1 (Asf1) is a highly conserved chaperone of histones H3/H4 that assembles or disassembles chromatin during transcription, replication, and repair. The structure of the globular domain of Asf1 bound to H3/H4 determined by X-ray crystallography to a resolution of 1.7 Angstroms shows how Asf1 binds the H3/H4 heterodimer, enveloping the C terminus of histone H3 and physically blocking formation of the H3/H4 heterotetramer. Unexpectedly, the C terminus of histone H4 that forms a mini-beta sheet with histone H2A in the nucleosome undergoes a major conformational change upon binding to Asf1 and adds a beta strand to the Asf1 beta sheet sandwich. Interactions with both H3 and H4 were required for Asf1 histone chaperone function in vivo and in vitro. The Asf1-H3/H4 structure suggests a "strand-capture" mechanism whereby the H4 tail acts as a lever to facilitate chromatin disassembly/assembly that may be used ubiquitously by histone chaperones.

PubMed: 17081973
DOI: 10.1016/j.cell.2006.08.047

Experimental method

X-RAY DIFFRACTION (1.7 Å)