1NLQ

The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding

Summary for 1NLQ

• Entry DOI: 10.2210/pdb1nlq/pdb
• Related: 1K5J
• Descriptor: Nucleoplasmin-like protein, MAGNESIUM ION (3 entities in total)
• Functional Keywords: dnlp, nucleoplasmin, chaperone, histone binding, ligand binding
• Biological source: Drosophila melanogaster (fruit fly)
• Cellular location: Nucleus: Q27415
• Total number of polymer chains: 5
• Total formula weight: 59900.54

Authors

Namboodiri, V.M.H.,Dutta, S.,Akey, I.V.,Head, J.F.,Akey, C.W. (deposition date: 2003-01-07, release date: 2003-03-01, Last modification date: 2024-02-14)

Primary citation

Namboodiri, V.M.H.,Dutta, S.,Akey, I.V.,Head, J.F.,Akey, C.W.
The crystal structure of Drosophila NLP-core Provides Insight into Pentamer Formation and Histone Binding
Structure, 11:175-186, 2003

PubMed Abstract: 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.

PubMed: 12575937
DOI: 10.1016/S0969-2126(03)00007-8

Experimental method

X-RAY DIFFRACTION (1.5 Å)