5h5f
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The crystal structure of the yeast arginine methyltransferase SFM1 complexed with SAM== |
| + | <StructureSection load='5h5f' size='340' side='right' caption='[[5h5f]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5h5f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H5F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H5F FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h5d|5h5d]], [[5h5e|5h5e]]</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=5h5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h5f OCA], [http://pdbe.org/5h5f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h5f RCSB], [http://www.ebi.ac.uk/pdbsum/5h5f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h5f ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Arginine methylation is a common post-translational modification and is critical for many cellular processes. Sfm1 is a novel arginine methyltransferase that contains a SpoU-TrmD (SPOUT) domain, a typical fold known for RNA methylation, but acts on a ribosomal protein. The underlying mechanism is poorly understood. Here, we report cocrystal structures of Sfm1 in complex with various ligands. We found that a critical loop responsible for S-adenosyl-l-methionine (SAM) binding adopts a different conformation from previous reports, and SAM appears to exhibit double conformations. Deletion of this loop greatly reduces the affinity of Sfm1 to SAM. Additionally, by comparison to closely related tRNA-methyltransferase Trm10, our structural analyses offer a good explanation why the two enzymes utilize distinct substrates, providing insights into the molecular mechanism. | ||
| - | + | A flexible cofactor-binding loop in the novel arginine methyltransferase Sfm1.,Wang C, Zeng J, Xie W FEBS Lett. 2016 Dec 19. doi: 10.1002/1873-3468.12533. PMID:27990635<ref>PMID:27990635</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5h5f" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Wang, C]] | ||
| + | [[Category: Xie, W]] | ||
| + | [[Category: Zeng, J]] | ||
| + | [[Category: Arginine methyltransferase]] | ||
| + | [[Category: Spout fold]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 16:22, 18 January 2017
The crystal structure of the yeast arginine methyltransferase SFM1 complexed with SAM
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