7w5m | pdb_00007w5m

Crystal structure of AtNASP in complex of H3 alpha3 helix peptide

spinqualitylabelsall models 7w5m, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7w5m is a 2 chain structure with sequence from Arabidopsis thaliana and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.15Å Ligands: GOL, PG4, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q94K88_ARATH Publication Abstract from PubMed The structural basis for histone recognition by the histone chaperone nuclear autoantigenic sperm protein (NASP) remains largely unclear. Here, we showed that Arabidopsis thaliana AtNASP is a monomer and displays robust nucleosome assembly activity in vitro. Examining the structure of AtNASP complexed with a histone H3 alpha3 peptide revealed a binding mode that is conserved in human NASP. AtNASP recognizes the H3 N-terminal region distinct from human NASP. Moreover, AtNASP forms a co-chaperone complex with ANTI-SILENCING FUNCTION 1 (ASF1) by binding to the H3 N-terminal region. Therefore, we deciphered the structure of AtNASP and the basis of the AtNASP-H3 interaction. Structural basis for histone H3 recognition by NASP in Arabidopsis.,Liu Y, Chen L, Wang N, Wu B, Bao H, Huang H J Integr Plant Biol. 2022 Dec;64(12):2309-2313. doi: 10.1111/jipb.13277. Epub , 2022 Jun 13. PMID:35587028 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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