1TZY
Crystal Structure of the Core-Histone Octamer to 1.90 Angstrom Resolution
Summary for 1TZY
Entry DOI | 10.2210/pdb1tzy/pdb |
Related | 1hq3 |
Descriptor | Histone H2A-IV, Histone H2B, HISTONE H3, ... (7 entities in total) |
Functional Keywords | histone-fold, tetramer-dimer-dimer, dna binding protein |
Biological source | Gallus gallus (chicken) More |
Cellular location | Nucleus: P02263 P84229 P62801 |
Total number of polymer chains | 8 |
Total formula weight | 110766.56 |
Authors | Wood, C.M.,Nicholson, J.M.,Chantalat, L.,Reynolds, C.D.,Lambert, S.J.,Baldwin, J.P. (deposition date: 2004-07-12, release date: 2004-08-03, Last modification date: 2024-03-13) |
Primary citation | Wood, C.M.,Nicholson, J.M.,Lambert, S.J.,Chantalat, L.,Reynolds, C.D.,Baldwin, J.P. High-resolution structure of the native histone octamer. Acta Crystallogr.,Sect.F, 61:541-545, 2005 Cited by PubMed Abstract: Crystals of native histone octamers (H2A-H2B)-(H4-H3)-(H3'-H4')-(H2B'-H2A') from chick erythrocytes in 2 M KCl, 1.35 M potassium phosphate pH 6.9 diffract X-rays to 1.90 A resolution, yielding a structure with an R(work) value of 18.7% and an Rfree of 22.2%. The crystal space group is P6(5), the asymmetric unit of which contains one complete octamer. This high-resolution model of the histone-core octamer allows further insight into intermolecular interactions, including water molecules, that dock the histone dimers to the tetramer in the nucleosome-core particle and have relevance to nucleosome remodelling. The three key areas analysed are the H2A'-H3-H4 molecular cluster (also H2A-H3'-H4'), the H4-H2B' interaction (also H4'-H2B) and the H2A'-H4 beta-sheet interaction (also H2A-H4'). The latter of these three regions is important to nucleosome remodelling by RNA polymerase II, as it is shown to be a likely core-histone binding site, and its disruption creates an instability in the nucleosome-core particle. A majority of the water molecules in the high-resolution octamer have positions that correlate to similar positions in the high-resolution nucleosome-core particle structure, suggesting that the high-resolution octamer model can be used for comparative studies with the high-resolution nucleosome-core particle. PubMed: 16511091DOI: 10.1107/S1744309105013813 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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