6WW4

Crystal structure of HERC2 ZZ domain in complex with histone H3 tail

Summary for 6WW4

• Entry DOI: 10.2210/pdb6ww4/pdb
• Descriptor: Histone H3.1,E3 ubiquitin-protein ligase HERC2, ZINC ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: zinc finger protein, histone reader, herc2, zz domain, gene regulation
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 13498.78

Authors

Liu, J.,Vann, K.R.,Kutateladze, T.G. (deposition date: 2020-05-07, release date: 2020-08-05, Last modification date: 2023-10-18)

Primary citation

Liu, J.,Xue, Z.,Zhang, Y.,Vann, K.R.,Shi, X.,Kutateladze, T.G.
Structural Insight into Binding of the ZZ Domain of HERC2 to Histone H3 and SUMO1.
Structure, 28:1225-1230.e3, 2020

PubMed Abstract: Human ubiquitin ligase HERC2, a component of the DNA repair machinery, has been linked to neurological diseases and cancer. Here, we show that the ZZ domain of HERC2 (HERC2) binds to histone H3 tail and tolerates posttranslational modifications commonly present in H3. The crystal structure of the HERC2:H3 complex provides the molecular basis for this interaction and highlights a critical role of the negatively charged site of HERC2 in capturing of A1 of H3. NMR, mutagenesis, and fluorescence data reveal that HERC2 binds to H3 and the N-terminal tail of SUMO1, a previously reported ligand of HERC2, with comparable affinities. Like H3, the N-terminal tail of SUMO1 occupies the same negatively charged site of HERC2 in the crystal structure of the complex, although in contrast to H3 it adopts an α-helical conformation. Our data suggest that HERC2 may play a role in mediating the association of HERC2 with chromatin.

PubMed: 32726574
DOI: 10.1016/j.str.2020.07.003

Experimental method

X-RAY DIFFRACTION (2.252 Å)