3C9C

Structural Basis of Histone H4 Recognition by p55

Summary for 3C9C

• Entry DOI: 10.2210/pdb3c9c/pdb
• Related: 3C99
• Descriptor: Chromatin assembly factor 1 p55 subunit, Histone H4, 27-residue peptide, CADMIUM ION (3 entities in total)
• Functional Keywords: p55, chromatin, epigenetics, wd4, histone, chromatin regulator, nucleus, phosphoprotein, repressor, transcription, transcription regulation, wd repeat, chromosomal protein, dna-binding, nucleosome core, nuclear protein, transcription repressor
• Biological source: Drosophila melanogaster (fruit fly); More
• Cellular location: Nucleus: Q24572 P84040
• Total number of polymer chains: 2
• Total formula weight: 52796.44

Authors

Song, J.J.,Garlick, J.D.,Kingston, R.E. (deposition date: 2008-02-15, release date: 2008-05-13, Last modification date: 2023-08-30)

Primary citation

Song, J.J.,Garlick, J.D.,Kingston, R.E.
Structural basis of histone H4 recognition by p55.
Genes Dev., 22:1313-1318, 2008

PubMed Abstract: p55 is a common component of many chromatin-modifying complexes and has been shown to bind to histones. Here, we present a crystal structure of Drosophila p55 bound to a histone H4 peptide. p55, a predicted WD40 repeat protein, recognizes the first helix of histone H4 via a binding pocket located on the side of a beta-propeller structure. The pocket cannot accommodate the histone fold of H4, which must be altered to allow p55 binding. Reconstitution experiments show that the binding pocket is important to the function of p55-containing complexes. These data demonstrate that WD40 repeat proteins use various surfaces to direct the modification of histones.

PubMed: 18443147
DOI: 10.1101/gad.1653308

Experimental method

X-RAY DIFFRACTION (3.2 Å)