3CFV

Structural basis of the interaction of RbAp46/RbAp48 with histone H4

Summary for 3CFV

• Entry DOI: 10.2210/pdb3cfv/pdb
• Related: 3CFS
• Descriptor: Histone-binding protein RBBP7, Histone H4 peptide, ARSENIC, ... (4 entities in total)
• Functional Keywords: rbap46/rbap48, chromatin, histone, wd-40 repeat protein, chaperone, flexib, chromatin regulator, dna replication, phosphoprotein, repressor, transcription, transcription regulation, wd repeat, chromosomal protein, dna-binding, nucleosome core, histone-chaperone complex, histone/chaperone
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q16576 P62805
• Total number of polymer chains: 4
• Total formula weight: 98574.87

Authors

Pei, X.-Y.,Murzina, N.V.,Zhang, W.,McLaughlin, S.,Verreault, A.,Luisi, B.F.,Laue, E.D. (deposition date: 2008-03-04, release date: 2008-06-10, Last modification date: 2024-04-03)

Primary citation

Murzina, N.V.,Pei, X.Y.,Zhang, W.,Sparkes, M.,Vicente-Garcia, J.,Pratap, J.V.,McLaughlin, S.H.,Ben-Shahar, T.R.,Verreault, A.,Luisi, B.F.,Laue, E.D.
Structural Basis for the Recognition of Histone H4 by the Histone-Chaperone RbAp46.
Structure, 16:1077-1085, 2008

PubMed Abstract: RbAp46 and RbAp48 (pRB-associated proteins p46 and p48, also known as RBBP7 and RBBP4, respectively) are highly homologous histone chaperones that play key roles in establishing and maintaining chromatin structure. We report here the crystal structure of human RbAp46 bound to histone H4. RbAp46 folds into a seven-bladed beta propeller structure and binds histone H4 in a groove formed between an N-terminal alpha helix and an extended loop inserted into blade six. Surprisingly, histone H4 adopts a different conformation when interacting with RbAp46 than it does in either the nucleosome or in the complex with ASF1, another histone chaperone. Our structural and biochemical results suggest that when a histone H3/H4 dimer (or tetramer) binds to RbAp46 or RbAp48, helix 1 of histone H4 unfolds to interact with the histone chaperone. We discuss the implications of our findings for the assembly and function of RbAp46 and RbAp48 complexes.

PubMed: 18571423
DOI: 10.1016/j.str.2008.05.006

Experimental method

X-RAY DIFFRACTION (2.6 Å)