7v6p | pdb_00007v6p

Crystal structure of human sNASP TPR domain

spinqualitylabelsall models 7v6p, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: CA, GOL, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Chromosomal duplication requires de novo assembly of nucleosomes from newly synthesized histones, and the process involves a dynamic network of interactions between histones and histone chaperones. sNASP and ASF1 are two major histone H3-H4 chaperones found in distinct and common complexes, yet how sNASP binds H3-H4 in the presence and absence of ASF1 remains unclear. Here we show that, in the presence of ASF1, sNASP principally recognizes a partially unfolded Nalpha region of histone H3, and in the absence of ASF1, an additional sNASP binding site becomes available in the core domain of the H3-H4 complex. Our study also implicates a critical role of the C-terminal tail of H4 in the transfer of H3-H4 between sNASP and ASF1 and the coiled-coil domain of sNASP in nucleosome assembly. These findings provide mechanistic insights into coordinated histone binding and transfer by histone chaperones. Distinct histone H3-H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones.,Liu CP, Jin W, Hu J, Wang M, Chen J, Li G, Xu RM Genes Dev. 2021 Dec 1;35(23-24):1610-1624. doi: 10.1101/gad.349100.121. Epub 2021, Nov 24. PMID:34819355 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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