5C74

Structure of a novel protein arginine methyltransferase

Summary for 5C74

• Entry DOI: 10.2210/pdb5c74/pdb
• Related: 5C77
• Descriptor: Protein arginine N-methyltransferase SFM1, SULFATE ION, NICKEL (II) ION, ... (4 entities in total)
• Functional Keywords: protein arginine methyltransferase, binging seites, s-adenosylhomocysteine, transferase
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 50147.96

Authors

Lv, F.,Ding, J. (deposition date: 2015-06-24, release date: 2016-01-13, Last modification date: 2024-03-20)

Primary citation

Lv, F.,Zhang, T.,Zhou, Z.,Gao, S.,Wong, C.C.,Zhou, J.Q.,Ding, J.
Structural basis for Sfm1 functioning as a protein arginine methyltransferase.
Cell Discov, 1:15037-15037, 2015

PubMed Abstract: 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.

PubMed: 27462434
DOI: 10.1038/celldisc.2015.37

Experimental method

X-RAY DIFFRACTION (1.9 Å)