2XYI
Crystal Structure of Nurf55 in complex with a H4 peptide
Summary for 2XYI
| Entry DOI | 10.2210/pdb2xyi/pdb |
| Related | 2PYO 3C99 3C9C |
| Descriptor | PROBABLE HISTONE-BINDING PROTEIN CAF1, HISTONE H4, TETRAETHYLENE GLYCOL, ... (5 entities in total) |
| Functional Keywords | transcription, repressor, phosphoprotein, wd-repeat |
| Biological source | DROSOPHILA MELANOGASTER (FRUIT FLY) More |
| Total number of polymer chains | 2 |
| Total formula weight | 51738.27 |
| Authors | Stirnimann, C.U.,Nowak, A.J.,Mueller, C.W. (deposition date: 2010-11-17, release date: 2011-05-04, Last modification date: 2023-12-20) |
| Primary citation | Nowak, A.J.,Alfieri, C.,Stirnimann, C.U.,Rybin, V.,Baudin, F.,Ly-Hartig, N.,Lindner, D.,Muller, C.W. Chromatin-Modifying Complex Component Nurf55/P55 Associates with Histones H3, H4 and Polycomb Repressive Complex 2 Subunit Su(Z)12 Through Partially Overlapping Binding Sites. J.Biol.Chem., 286:23388-, 2011 Cited by PubMed Abstract: Drosophila Nurf55 is a component of different chromatin-modifying complexes, including the PRC2 (Polycomb repressive complex 2). Based on the 1.75-Å crystal structure of Nurf55 bound to histone H4 helix 1, we analyzed interactions of Nurf55 (Nurf55 or p55 in fly and RbAp48/46 in human) with the N-terminal tail of histone H3, the first helix of histone H4, and an N-terminal fragment of the PRC2 subunit Su(z)12 using isothermal calorimetry and pulldown experiments. Site-directed mutagenesis identified the binding site of histone H3 at the top of the Nurf55 WD40 propeller. Unmodified or K9me3- or K27me3-containing H3 peptides were bound with similar affinities, whereas the affinity for K4me3-containing H3 peptides was reduced. Helix 1 of histone H4 and Su(z)12 bound to the edge of the β-propeller using overlapping binding sites. Our results show similarities in the recognition of histone H4 and Su(z)12 and identify Nurf55 as a versatile interactor that simultaneously contacts multiple partners. PubMed: 21550984DOI: 10.1074/JBC.M110.207407 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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