Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Protein methylation at arginines is ubiquitous in eukaryotes and affects signal transduction, gene expression and protein sorting. Hmt1/Rmt1, the major arginine methyltransferase in yeast, catalyzes methylation of arginine residues in several mRNA-binding proteins and facilitates their export from the nucleus. We now report the crystal structure of Hmt1 at 2.9 A resolution. Hmt1 forms a hexamer with approximate 32 symmetry. The surface of the oligomer is dominated by large acidic cavities at the dimer interfaces. Mutation of dimer contact sites eliminates activity of Hmt1 both in vivo and in vitro. Mutating residues in the acidic cavity significantly reduces binding and methylation of the substrate Npl3.
The structure and oligomerization of the yeast arginine methyltransferase, Hmt1.,Weiss VH, McBride AE, Soriano MA, Filman DJ, Silver PA, Hogle JM Nat Struct Biol. 2000 Dec;7(12):1165-71. PMID:11101900[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Weiss VH, McBride AE, Soriano MA, Filman DJ, Silver PA, Hogle JM. The structure and oligomerization of the yeast arginine methyltransferase, Hmt1. Nat Struct Biol. 2000 Dec;7(12):1165-71. PMID:11101900 doi:10.1038/82028
