5h5f | pdb_00005h5f

The crystal structure of the yeast arginine methyltransferase SFM1 complexed with SAM

spinqualitylabelsall models 5h5f, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5h5f is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: SAM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SFM1_YEAST S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that monomethylates ribosomal protein S3 (RPS3) at 'Arg-146'. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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