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1K5J

The Crystal Structure of Nucleoplasmin-Core

Summary for 1K5J
Entry DOI10.2210/pdb1k5j/pdb
DescriptorNucleoplasmin Core (2 entities in total)
Functional Keywordsbeta-barrel, jellyroll, beta-bulge, pentamer, chaperone
Biological sourceXenopus laevis (African clawed frog)
Cellular locationNucleus: P05221
Total number of polymer chains5
Total formula weight68763.42
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 citationDutta, 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: 11684019
DOI: 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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