7W5M

Crystal structure of AtNASP in complex of H3 alpha3 helix peptide

Summary for 7W5M

• Entry DOI: 10.2210/pdb7w5m/pdb
• Descriptor: Tetratricopeptide repeat (TPR)-like superfamily protein, H3 alpha3 helix peptide, GLYCEROL, ... (6 entities in total)
• Functional Keywords: histone chaperone, chaperone
• Biological source: Arabidopsis thaliana (thale cress); More
• Total number of polymer chains: 2
• Total formula weight: 32723.69

Authors

Liu, Y.,Bao, H. (deposition date: 2021-11-30, release date: 2022-05-18, Last modification date: 2023-11-29)

Primary citation

Liu, Y.,Chen, L.,Wang, N.,Wu, B.,Bao, H.,Huang, H.
Structural basis for histone H3 recognition by NASP in Arabidopsis.
J Integr Plant Biol, 64:2309-2313, 2022

PubMed Abstract: 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 α3 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.

PubMed: 35587028
DOI: 10.1111/jipb.13277

Experimental method

X-RAY DIFFRACTION (2.15 Å)