1XE0

The structure and function of Xenopus NO38-core, a histone binding chaperone in the nucleolus

Summary for 1XE0

• Entry DOI: 10.2210/pdb1xe0/pdb
• Related: 1K5J 1NLQ 1XB9
• Descriptor: Nucleophosmin (2 entities in total)
• Functional Keywords: no38, drosophila nucleoplasmin-like protein (dnlp), nucleoplasmin (np), histone binding, chaperone
• Biological source: Xenopus laevis (African clawed frog)
• Cellular location: Cytoplasm (By similarity): P07222
• Total number of polymer chains: 10
• Total formula weight: 123519.86

Authors

Namboodiri, V.M.,Akey, I.V.,Schmidt-Zachmann, M.S.,Head, J.F.,Akey, C.W. (deposition date: 2004-09-08, release date: 2004-12-21, Last modification date: 2023-08-23)

Primary citation

Namboodiri, V.M.,Akey, I.V.,Schmidt-Zachmann, M.S.,Head, J.F.,Akey, C.W.
The Structure and Function of Xenopus NO38-Core, a Histone Chaperone in the Nucleolus.
Structure, 12:2149-2160, 2004

PubMed Abstract: Xenopus NO38 is an abundant nucleolar chaperone and a member of the nucleoplasmin (Np) family. Here, we report high-resolution crystal structures of the N-terminal domain of NO38, as a pentamer and a decamer. As expected, NO38 shares the Np family fold. In addition, NO38- and Np-core pentamers each use highly conserved residues and numerous waters to form their respective decamers. Further studies show that NO38 and Np each bind equal amounts of the four core histones. However, NO38 prefers the (H3-H4)(2) tetramer, while Np probably prefers H2A-H2B dimers. We also show that NO38 and Np will each bind noncognate histones when the preferred partner is absent. We suggest that these chaperones must form decamers in order to bind histones and differentiate between histone tetramers and dimers. When taken together, these data imply that NO38 may function as a histone chaperone in the nucleolus.

PubMed: 15576029
DOI: 10.1016/j.str.2004.09.017

Experimental method

X-RAY DIFFRACTION (1.7 Å)