Structural highlights
Function
[TRMY_METJA] Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs.[HAMAP-Rule:MF_00587][1] [2]
Publication Abstract from PubMed
The proteins in DUF358 family are all bacterial proteins, which are approximately 200 amino acids long with unknown function. Bioinformatics analysis suggests that these proteins contain several conserved arginines and aspartates that might adopt SPOUT-class fold. Here we report crystal structure of Methanocaldococcus jannaschii DUF358/Mj1640 in complex with S-adenosyl-L-methionine (SAM) at 1.4 A resolution. The structure reveals a single domain structure consisting of eight-stranded beta-sheets sandwiched by six alpha-helices at both sides. Similar to other SPOUT-class members, Mj1640 contains a typical deep trefoil knot at its C-terminus to accommodate the SAM cofactor. However, Mj1640 has limited structural extension at its N-terminus, which is unique to this family member. Mj1640 forms a dimer, which is mediated by two parallel pairs of alpha-helices oriented almost perpendicular to each other. Although Mj1640 shares close structural similarity with Nep1, the significant differences in N-terminal extension domain and the overall surface charge distribution strongly suggest that Mj1640 might target a different RNA sequence. Detailed structural analysis of the SAM-binding pocket reveals that Asp157 or Glu183 from its own monomer or Ser43 from the associate monomer probably plays the catalytic role for RNA methylation.
Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase.,Chen HY, Yuan YA J Mol Cell Biol. 2010 Dec;2(6):366-74. PMID:21098051[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chatterjee K, Blaby IK, Thiaville PC, Majumder M, Grosjean H, Yuan YA, Gupta R, de Crecy-Lagard V. The archaeal COG1901/DUF358 SPOUT-methyltransferase members, together with pseudouridine synthase Pus10, catalyze the formation of 1-methylpseudouridine at position 54 of tRNA. RNA. 2012 Mar;18(3):421-33. doi: 10.1261/rna.030841.111. Epub 2012 Jan 24. PMID:22274953 doi:http://dx.doi.org/10.1261/rna.030841.111
- ↑ Wurm JP, Griese M, Bahr U, Held M, Heckel A, Karas M, Soppa J, Wohnert J. Identification of the enzyme responsible for N1-methylation of pseudouridine 54 in archaeal tRNAs. RNA. 2012 Mar;18(3):412-20. doi: 10.1261/rna.028498.111. Epub 2012 Jan 24. PMID:22274954 doi:http://dx.doi.org/10.1261/rna.028498.111
- ↑ Chen HY, Yuan YA. Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase. J Mol Cell Biol. 2010 Dec;2(6):366-74. PMID:21098051 doi:10.1093/jmcb/mjq034
