1g6q
From Proteopedia
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<StructureSection load='1g6q' size='340' side='right'caption='[[1g6q]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='1g6q' size='340' side='right'caption='[[1g6q]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1g6q]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1g6q]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G6Q FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g6q OCA], [https://pdbe.org/1g6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g6q RCSB], [https://www.ebi.ac.uk/pdbsum/1g6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g6q ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g6q OCA], [https://pdbe.org/1g6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g6q RCSB], [https://www.ebi.ac.uk/pdbsum/1g6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g6q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/HMT1_YEAST HMT1_YEAST] Methylates arginines in a variety of RNA-binding proteins. Methylates NOP3. Can catalyze both the mono- and asymmetric dimethylation. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1g6q ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1g6q ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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. | ||
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| - | 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<ref>PMID:11101900</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1g6q" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: | + | [[Category: Filman DJ]] |
| - | [[Category: | + | [[Category: Hogle JM]] |
| - | [[Category: | + | [[Category: McBride AE]] |
| - | [[Category: | + | [[Category: Silver PA]] |
| - | [[Category: | + | [[Category: Soriano MA]] |
| - | [[Category: | + | [[Category: Weiss VH]] |
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Current revision
CRYSTAL STRUCTURE OF YEAST ARGININE METHYLTRANSFERASE, HMT1
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