1g6q

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{{STRUCTURE_1g6q| PDB=1g6q | SCENE= }}
{{STRUCTURE_1g6q| PDB=1g6q | SCENE= }}
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'''CRYSTAL STRUCTURE OF YEAST ARGININE METHYLTRANSFERASE, HMT1'''
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===CRYSTAL STRUCTURE OF YEAST ARGININE METHYLTRANSFERASE, HMT1===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11101900 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11101900}}
==About this Structure==
==About this Structure==
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[[Category: Mixed alpha-beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:45:42 2008''

Revision as of 01:45, 1 July 2008

Image:1g6q.png

Template:STRUCTURE 1g6q

CRYSTAL STRUCTURE OF YEAST ARGININE METHYLTRANSFERASE, HMT1

Template:ABSTRACT PUBMED 11101900

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

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