5WVO

Crystal structure of DNMT1 RFTS domain in complex with K18/K23 mono-ubiquitylated histone H3

Summary for 5WVO

• Entry DOI: 10.2210/pdb5wvo/pdb
• Descriptor: Ubiquitin, DNA (cytosine-5)-methyltransferase 1, Histone H3.1, ... (5 entities in total)
• Functional Keywords: dna methylation, ubiquitination, signaling protein-transferase complex, signaling protein/transferase
• Biological source: Homo sapiens (Human); More
• Cellular location: Ubiquitin: Cytoplasm : P62979; Nucleus : P26358 P68431
• Total number of polymer chains: 4
• Total formula weight: 49116.05

Authors

Ishiyama, S.,Nishiyama, A.,Nakanishi, M.,Arita, K. (deposition date: 2016-12-28, release date: 2017-11-15, Last modification date: 2023-11-22)

• Primary citation: Ishiyama, S.,Nishiyama, A.,Saeki, Y.,Moritsugu, K.,Morimoto, D.,Yamaguchi, L.,Arai, N.,Matsumura, R.,Kawakami, T.,Mishima, Y.,Hojo, H.,Shimamura, S.,Ishikawa, F.,Tajima, S.,Tanaka, K.,Ariyoshi, M.,Shirakawa, M.,Ikeguchi, M.,Kidera, A.,Suetake, I.,Arita, K.,Nakanishi, M.; Structure of the Dnmt1 Reader Module Complexed with a Unique Two-Mono-Ubiquitin Mark on Histone H3 Reveals the Basis for DNA Methylation Maintenance; Mol. Cell, 68:350-360.e7, 2017; PubMed: 29053958; DOI: 10.1016/j.molcel.2017.09.037

Experimental method

X-RAY DIFFRACTION (1.997 Å)