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
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[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
- ↑ Wang C, Zeng J, Xie W. A flexible cofactor-binding loop in the novel arginine methyltransferase Sfm1. FEBS Lett. 2016 Dec 19. doi: 10.1002/1873-3468.12533. PMID:27990635 doi:http://dx.doi.org/10.1002/1873-3468.12533
