5c77: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<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> | <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" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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='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='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> | ||
</table> | </table> | ||
Latest revision as of 19:07, 8 November 2023
A novel protein arginine methyltransferaseA novel protein arginine methyltransferase
Structural highlights
FunctionSFM1_YEAST S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that monomethylates ribosomal protein S3 (RPS3) at 'Arg-146'.[1] Publication Abstract from PubMedSPOUT 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
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