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1xe0
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(New page: 200px<br /><applet load="1xe0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xe0, resolution 1.70Å" /> '''The structure and fu...)
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Revision as of 03:53, 21 November 2007
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The structure and function of Xenopus NO38-core, a histone binding chaperone in the nucleolus
Overview
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.
About this Structure
1XE0 is a Single protein structure of sequence from Xenopus laevis. Full crystallographic information is available from OCA.
Reference
The structure and function of Xenopus NO38-core, a histone chaperone in the nucleolus., Namboodiri VM, Akey IV, Schmidt-Zachmann MS, Head JF, Akey CW, Structure. 2004 Dec;12(12):2149-60. PMID:15576029
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