9V17

Crystal structure of E. coli glycogen phosphorylase N185A/R267E mutant

Summary for 9V17

• Entry DOI: 10.2210/pdb9v17/pdb
• Descriptor: Glycogen phosphorylase (1 entity in total)
• Functional Keywords: glycogen phosphorylase, transferase
• Biological source: Escherichia coli K12
• Total number of polymer chains: 4
• Total formula weight: 374506.25

Authors

Takai, M.,Shobu, K.,Fukuda, Y.,Inoue, T. (deposition date: 2025-05-19, release date: 2026-02-18, Last modification date: 2026-03-04)

Primary citation

Kujirai, T.,Ehara, H.,Ito, T.,Henmi, M.,Oya, E.,Kobayashi, T.,Sekine, S.I.,Kurumizaka, H.
Structural basis of transcription-coupled H3K36 trimethylation by Set2 in coordination with FACT.
Sci Adv, 12:eaed1952-eaed1952, 2026

PubMed Abstract: Trimethylation of the histone H3K36 residue (H3K36me3) plays an indispensable role in ensuring transcription fidelity by suppressing undesired cryptic transcription in chromatin. H3K36me3 modification is accomplished by Set2/SETD2 during transcription elongation by the RNA polymerase II elongation complex (EC). Here, we found that Set2-mediated H3K36me3 deposition occurs on the nucleosome reassembling behind the EC. The histone chaperone FACT suppresses H3K36me3 deposition on the downstream nucleosome, thereby ensuring that Set2 targets specifically on the reassembling upstream nucleosome. Cryo-electron microscopy structures of the nucleosome-transcribing EC complexed with Set2 revealed that Set2 is anchored by the Spt6 subunit of the EC to capture both of the H3 N-terminal tails in a stepwise manner during the nucleosome reassembly process. Abrogation of the Set2-EC interaction leads to defective transcription-coupled H3K36me3 deposition. These insights elucidate the structure-based mechanism of transcription-coupled H3K36me3 deposition in chromatin.

PubMed: 41604494
DOI: 10.1126/sciadv.aed1952

Experimental method

X-RAY DIFFRACTION (3.7 Å)