2xql | pdb_00002xql

Fitting of the H2A-H2B histones in the electron microscopy map of the complex Nucleoplasmin:H2A-H2B histones (1:5).

spinqualitylabelsall models 2xql, resolution 19.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xql is a 10 chain structure with sequence from Chick. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2hio, 1tzy, 1hq3, 2aro, 1hio, 1eqz Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Nucleoplasmin (NP) is a pentameric chaperone that regulates the condensation state of chromatin extracting specific basic proteins from sperm chromatin and depositing H2A-H2B histone dimers. It has been proposed that histones could bind to either the lateral or distal face of the pentameric structure. Here, we combine different biochemical and biophysical techniques to show that natural, hyperphosphorylated NP can bind five H2A-H2B dimers and that the amount of bound ligand depends on the overall charge (phosphorylation level) of the chaperone. Three-dimensional reconstruction of NP/H2A-H2B complex carried out by electron microscopy reveals that histones interact with the chaperone distal face. Limited proteolysis and mass spectrometry indicate that the interaction results in protection of the histone fold and most of the H2A and H2B C-terminal tails. This structural information can help to understand the function of NP as a histone chaperone. Nucleoplasmin binds histone H2A-H2B dimers through its distal face.,Ramos I, Martin-Benito J, Finn R, Bretana L, Aloria K, Arizmendi JM, Ausio J, Muga A, Valpuesta JM, Prado A J Biol Chem. 2010 Oct 29;285(44):33771-8. Epub 2010 Aug 9. PMID:20696766 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Histone

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