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| | <StructureSection load='5c77' size='340' side='right'caption='[[5c77]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5c77' size='340' side='right'caption='[[5c77]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5c77]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C77 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C77 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5c77]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C77 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c74|5c74]]</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=5c77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c77 OCA], [https://pdbe.org/5c77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c77 RCSB], [https://www.ebi.ac.uk/pdbsum/5c77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c77 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SFM1, YOR021C, OR26.11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5c77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c77 OCA], [http://pdbe.org/5c77 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c77 RCSB], [http://www.ebi.ac.uk/pdbsum/5c77 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c77 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SFM1_YEAST SFM1_YEAST]] S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that monomethylates ribosomal protein S3 (RPS3) at 'Arg-146'.<ref>PMID:22650761</ref> | + | [https://www.uniprot.org/uniprot/SFM1_YEAST SFM1_YEAST] S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that monomethylates ribosomal protein S3 (RPS3) at 'Arg-146'.<ref>PMID:22650761</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ding, J]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Lv, F]] | + | [[Category: Ding J]] |
| - | [[Category: Zhang, T]] | + | [[Category: Lv F]] |
| - | [[Category: Arginine]] | + | [[Category: Zhang T]] |
| - | [[Category: Protein arginine methyltransferase]]
| + | |
| - | [[Category: Sah]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Yeast]]
| + | |
| Structural highlights
Function
SFM1_YEAST S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that monomethylates ribosomal protein S3 (RPS3) at 'Arg-146'.[1]
Publication Abstract from PubMed
SPOUT proteins constitute one class of methyltransferases, which so far are found to exert activity mainly towards RNAs. Previously, yeast Sfm1 was predicted to contain a SPOUT domain but can methylate ribosomal protein S3. Here we report the crystal structure of Sfm1, which comprises of a typical SPOUT domain and a small C-terminal domain. The active site is similar to that of protein arginine methyltransferases but different from that of RNA methyltransferases. In addition, Sfm1 exhibits a negatively charged surface surrounding the active site unsuitable for RNA binding. Our biochemical data show that Sfm1 exists as a monomer and has high activity towards ribosomal protein S3 but no activity towards RNA. It can specifically catalyze the methylation of Arg146 of S3 and the C-terminal domain is critical for substrate binding and activity. These results together provide the structural basis for Sfm1 functioning as a PRMT for ribosomal protein S3.
Structural basis for Sfm1 functioning as a protein arginine methyltransferase.,Lv F, Zhang T, Zhou Z, Gao S, Wong CC, Zhou JQ, Ding J Cell Discov. 2015 Dec 29;1:15037. doi: 10.1038/celldisc.2015.37. eCollection, 2015. PMID:27462434[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Young BD, Weiss DI, Zurita-Lopez CI, Webb KJ, Clarke SG, McBride AE. Identification of methylated proteins in the yeast small ribosomal subunit: a role for SPOUT methyltransferases in protein arginine methylation. Biochemistry. 2012 Jun 26;51(25):5091-104. doi: 10.1021/bi300186g. Epub 2012 Jun , 15. PMID:22650761 doi:http://dx.doi.org/10.1021/bi300186g
- ↑ Lv F, Zhang T, Zhou Z, Gao S, Wong CC, Zhou JQ, Ding J. Structural basis for Sfm1 functioning as a protein arginine methyltransferase. Cell Discov. 2015 Dec 29;1:15037. doi: 10.1038/celldisc.2015.37. eCollection, 2015. PMID:27462434 doi:http://dx.doi.org/10.1038/celldisc.2015.37
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