1g6q
From Proteopedia
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'''CRYSTAL STRUCTURE OF YEAST ARGININE METHYLTRANSFERASE, HMT1''' | '''CRYSTAL STRUCTURE OF YEAST ARGININE METHYLTRANSFERASE, HMT1''' | ||
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[[Category: Soriano, M A.]] | [[Category: Soriano, M A.]] | ||
[[Category: Weiss, V H.]] | [[Category: Weiss, V H.]] | ||
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Revision as of 14:12, 2 May 2008
CRYSTAL STRUCTURE OF YEAST ARGININE METHYLTRANSFERASE, HMT1
Overview
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.
About this Structure
1G6Q is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 17:12:30 2008
