4BUP

A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases

Summary for 4BUP

• Entry DOI: 10.2210/pdb4bup/pdb
• Related: 4AU7
• Descriptor: HISTONE-LYSINE N-METHYLTRANSFERASE SUV420H1, ZINC ION, S-ADENOSYLMETHIONINE, ... (5 entities in total)
• Functional Keywords: transferase, epigenetics, histone
• Biological source: MUS MUSCULUS (HOUSE MOUSE)
• Cellular location: Nucleus: Q3U8K7
• Total number of polymer chains: 2
• Total formula weight: 63482.58

Authors

Southall, S.M.,Cronin, N.B.,Wilson, J.R. (deposition date: 2013-06-21, release date: 2013-10-02, Last modification date: 2023-12-20)

Primary citation

Southall, S.M.,Cronin, N.B.,Wilson, J.R.
A Novel Route to Product Specificity in the Suv4-20 Family of Histone H4K20 Methyltransferases.
Nucleic Acids Res., 42:661-, 2014

PubMed Abstract: The delivery of site-specific post-translational modifications to histones generates an epigenetic regulatory network that directs fundamental DNA-mediated processes and governs key stages in development. Methylation of histone H4 lysine-20 has been implicated in DNA repair, transcriptional silencing, genomic stability and regulation of replication. We present the structure of the histone H4K20 methyltransferase Suv4-20h2 in complex with its histone H4 peptide substrate and S-adenosyl methionine cofactor. Analysis of the structure reveals that the Suv4-20h2 active site diverges from the canonical SET domain configuration and generates a high degree of both substrate and product specificity. Together with supporting biochemical data comparing Suv4-20h1 and Suv4-20h2, we demonstrate that the Suv4-20 family enzymes take a previously mono-methylated H4K20 substrate and generate an exclusively di-methylated product. We therefore predict that other enzymes are responsible for the tri-methylation of histone H4K20 that marks silenced heterochromatin.

PubMed: 24049080
DOI: 10.1093/NAR/GKT776

Experimental method

X-RAY DIFFRACTION (2.166 Å)