6ww4

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

spinqualitylabelsall models 6ww4, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ww4 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.252Å Ligands: GOL, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HERC2_HUMAN E3 ubiquitin-protein ligase that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. Recruited to sites of DNA damage in response to ionizing radiation (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA damage-induced formation of 'Lys-63'-linked ubiquitin chains. Acts as a mediator of binding specificity between UBE2N and RNF8. Involved in the maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of XPA which influences the circadian oscillation of DNA excision repair activity. H31_HUMAN Publication Abstract from PubMed 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 (HERC2ZZ) binds to histone H3 tail and tolerates posttranslational modifications commonly present in H3. The crystal structure of the HERC2ZZ:H3 complex provides the molecular basis for this interaction and highlights a critical role of the negatively charged site of HERC2ZZ in capturing of A1 of H3. NMR, mutagenesis, and fluorescence data reveal that HERC2ZZ binds to H3 and the N-terminal tail of SUMO1, a previously reported ligand of HERC2ZZ, with comparable affinities. Like H3, the N-terminal tail of SUMO1 occupies the same negatively charged site of HERC2ZZ in the crystal structure of the complex, although in contrast to H3 it adopts an alpha-helical conformation. Our data suggest that HERC2ZZ may play a role in mediating the association of HERC2 with chromatin. Structural Insight into Binding of the ZZ Domain of HERC2 to Histone H3 and SUMO1.,Liu J, Xue Z, Zhang Y, Vann KR, Shi X, Kutateladze TG Structure. 2020 Jul 23. pii: S0969-2126(20)30236-7. doi:, 10.1016/j.str.2020.07.003. PMID:32726574 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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