1nlq | pdb_00001nlq

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

spinqualitylabelsall models 1nlq, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1nlq is a 5 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG Related: 1k5j Gene: NLP OR CRP1 OR CG7917 (Drosophila melanogaster) Resources: FirstGlance, OCA, RCSB, PDBsum 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 PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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