1K5J
The Crystal Structure of Nucleoplasmin-Core
Summary for 1K5J
| Entry DOI | 10.2210/pdb1k5j/pdb |
| Descriptor | Nucleoplasmin Core (2 entities in total) |
| Functional Keywords | beta-barrel, jellyroll, beta-bulge, pentamer, chaperone |
| Biological source | Xenopus laevis (African clawed frog) |
| Cellular location | Nucleus: P05221 |
| Total number of polymer chains | 5 |
| Total formula weight | 68763.42 |
| Authors | Dutta, S.,Akey, I.V.,Dingwall, C.,Hartman, K.L.,Laue, T.,Nolte, R.T.,Head, J.F.,Akey, C.W. (deposition date: 2001-10-10, release date: 2001-11-01, Last modification date: 2024-02-07) |
| Primary citation | Dutta, S.,Akey, I.V.,Dingwall, C.,Hartman, K.L.,Laue, T.,Nolte, R.T.,Head, J.F.,Akey, C.W. The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly. Mol.Cell, 8:841-853, 2001 Cited by PubMed Abstract: The efficient assembly of histone complexes and nucleosomes requires the participation of molecular chaperones. Currently, there is a paucity of data on their mechanism of action. We now present the structure of an N-terminal domain of nucleoplasmin (Np-core) at 2.3 A resolution. The Np-core monomer is an eight-stranded beta barrel that fits snugly within a stable pentamer. In the crystal, two pentamers associate to form a decamer. We show that both Np and Np-core are competent to assemble large complexes that contain the four core histones. Further experiments and modeling suggest that these complexes each contain five histone octamers which dock to a central Np decamer. This work has important ramifications for models of histone storage, sperm chromatin decondensation, and nucleosome assembly. PubMed: 11684019DOI: 10.1016/S1097-2765(01)00354-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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