1ML9

Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase

Summary for 1ML9

• Entry DOI: 10.2210/pdb1ml9/pdb
• Descriptor: Histone H3 methyltransferase DIM-5, ZINC ION, UNKNOWN, ... (4 entities in total)
• Functional Keywords: dim-5, adomet-dependent methyltransferase histone h3 lysine-9 methylation, transferase
• Biological source: Neurospora crassa
• Total number of polymer chains: 1
• Total formula weight: 34926.50

Authors

Zhang, X.,Tamaru, H.,Khan, S.I.,Horton, J.R.,Keefe, L.J.,Selker, E.U.,Cheng, X. (deposition date: 2002-08-30, release date: 2002-10-23, Last modification date: 2024-02-14)

Primary citation

Zhang, X.,Tamaru, H.,Khan, S.I.,Horton, J.R.,Keefe, L.J.,Selker, E.U.,Cheng, X.
Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase
Cell(Cambridge,Mass.), 111:117-127, 2002

PubMed Abstract: AdoMet-dependent methylation of histones is part of the "histone code" that can profoundly influence gene expression. We describe the crystal structure of Neurospora DIM-5, a histone H3 lysine 9 methyltranferase (HKMT), determined at 1.98 A resolution, as well as results of biochemical characterization and site-directed mutagenesis of key residues. This SET domain protein bears no structural similarity to previously characterized AdoMet-dependent methyltransferases but includes notable features such as a triangular Zn3Cys9 zinc cluster in the pre-SET domain and a AdoMet binding site in the SET domain essential for methyl transfer. The structure suggests a mechanism for the methylation reaction and provides the structural basis for functional characterization of the HKMT family and the SET domain.

PubMed: 12372305
DOI: 10.1016/S0092-8674(02)00999-6

Experimental method

X-RAY DIFFRACTION (1.98 Å)