1g6q

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|ACTIVITY=
|ACTIVITY=
|GENE= HMT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|GENE= HMT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g6q OCA], [http://www.ebi.ac.uk/pdbsum/1g6q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g6q RCSB]</span>
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[[Category: sam-binding domain]]
[[Category: sam-binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:37:52 2008''

Revision as of 17:37, 30 March 2008


PDB ID 1g6q

Drag the structure with the mouse to rotate
, resolution 2.90Å
Gene: HMT1 (Saccharomyces cerevisiae)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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