1MT6

Structure of histone H3 K4-specific methyltransferase SET7/9 with AdoHcy

Summary for 1MT6

• Entry DOI: 10.2210/pdb1mt6/pdb
• Related: 1MUF
• Descriptor: SET9, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• Functional Keywords: set domain, histone lysine methyltransferase, adohcy, knot, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q8WTS6
• Total number of polymer chains: 1
• Total formula weight: 31534.82

Authors

Jacobs, S.A.,Harp, J.M.,Devarakonda, S.,Kim, Y.,Rastinejad, F.,Khorasanizadeh, S. (deposition date: 2002-09-20, release date: 2002-11-06, Last modification date: 2024-02-14)

Primary citation

Jacobs, S.A.,Harp, J.M.,Devarakonda, S.,Kim, Y.,Rastinejad, F.,Khorasanizadeh, S.
The active site of the SET domain is constructed on a knot
Nat.Struct.Biol., 9:833-838, 2002

PubMed Abstract: The SET domain contains the catalytic center of lysine methyltransferases that target the N-terminal tails of histones and regulate chromatin function. Here we report the structure of the SET7/9 protein in the absence and presence of its cofactor product, S-adenosyl-L-homocysteine (AdoHcy). A knot within the SET domain helps form the methyltransferase active site, where AdoHcy binds and lysine methylation is likely to occur. A structure-guided comparison of sequences within the SET protein family suggests that the knot substructure and active site environment are conserved features of the SET domain.

PubMed: 12389038

Experimental method

X-RAY DIFFRACTION (2.2 Å)