1nlq
From Proteopedia
The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding
Structural highlights
Function[NLP_DROME] Binds to core histones and functions in the ATP-facilitated assembly of approximately regularly spaced nucleosomal arrays. May participate in parallel with other histone-binding proteins such as NAP-1.[1] [2] Isoform 2 is inactive for chromatin assembly. In vitro it appears to form a high molecular mass aggregate with the core histones.[3] [4] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Drome | Akey, C W | Akey, I V | Dutta, S | Head, J F | Namboodiri, V M.H | Chaperone | Dnlp | Histone binding | Ligand binding | Nucleoplasmin
