3S8P

Crystal Structure of the SET Domain of Human Histone-Lysine N-Methyltransferase SUV420H1 In Complex With S-Adenosyl-L-Methionine

Summary for 3S8P

• Entry DOI: 10.2210/pdb3s8p/pdb
• Descriptor: Histone-lysine N-methyltransferase SUV420H1, ZINC ION, S-ADENOSYLMETHIONINE, ... (4 entities in total)
• Functional Keywords: set domain, histone methyltransferase, transcription regulation, histone lysine, sam, methylation, nucleus, chromosome, structural genomics, structural genomics consortium, sgc, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : Q4FZB7
• Total number of polymer chains: 2
• Total formula weight: 64689.94

Authors

Lam, R.,Zeng, H.,Loppnau, P.,Bountra, C.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Wu, H.,Structural Genomics Consortium (SGC) (deposition date: 2011-05-30, release date: 2011-07-06, Last modification date: 2024-11-20)

Primary citation

Wu, H.,Siarheyeva, A.,Zeng, H.,Lam, R.,Dong, A.,Wu, X.H.,Li, Y.,Schapira, M.,Vedadi, M.,Min, J.
Crystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2.
Febs Lett., 587:3859-3868, 2013

PubMed Abstract: SUV420H1 and SUV420H2 are two highly homologous enzymes that methylate lysine 20 of histone H4 (H4K20), a mark that has been implicated in transcriptional regulation. In this study, we present the high-resolution crystal structures of human SUV420H1 and SUV420H2 in complex with SAM, and report their substrate specificity. Both methyltransferases have a unique N-terminal domain and Zn-binding post-SET domain, and prefer the monomethylated histone H4K20 as a substrate in vitro. No histone H4K20 trimethylation activity was detected by our radioactivity-based assay for either enzyme, consistent with the presence of a conserved serine residue that forms a hydrogen bond with the target lysine side-chain and limits the methylation level.

PubMed: 24396869

Experimental method

X-RAY DIFFRACTION (1.85 Å)