1nlq
From Proteopedia
| |||||||
| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | NLP OR CRP1 OR CG7917 (Drosophila melanogaster) | ||||||
| Related: | 1K5J
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding
Overview
The nucleoplasmin-like protein from Drosophila (dNLP) functions as a chaperone for core histones and may remodel chromatin in embryos. We now report the crystal structure of a dNLP-core pentamer at 1.5 A resolution. The monomer has an eight-stranded, beta barrel topology that is similar to nucleoplasmin (Np). However, a signature beta hairpin is tucked in along the lateral surface of the dNLP-core pentamer, while it extends outward in the Np-core decamer. Drosophila NLP and Np both assemble histone octamers. This process may require each chaperone to form a decamer, which would create symmetric binding sites for the histones. Conformational differences between dNLP and Np may reflect their different oligomeric states, while a conserved, nonpolar subunit interface may allow conformational plasticity during histone binding.
About this Structure
1NLQ is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding., Namboodiri VM, Dutta S, Akey IV, Head JF, Akey CW, Structure. 2003 Feb;11(2):175-86. PMID:12575937
Page seeded by OCA on Sun Mar 30 22:32:07 2008
