Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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.

Original publication

DOI

10.1038/nsb861

Type

Journal article

Journal

Nature structural biology

Publication Date

11/2002

Volume

9

Pages

833 - 838

Addresses

Department of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, Virginia 22908, USA.

Keywords

Humans, Coenzymes, Methyltransferases, Protein Methyltransferases, Histone-Lysine N-Methyltransferase, S-Adenosylhomocysteine, Recombinant Proteins, Crystallography, X-Ray, Magnetic Resonance Spectroscopy, Sequence Alignment, Binding Sites, Amino Acid Sequence, Conserved Sequence, Protein Structure, Secondary, Protein Structure, Tertiary, Models, Molecular, Molecular Sequence Data, Histone Methyltransferases