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|Title:||Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase|
SPOUT-class RNA methyltransferase
|Citation:||Chen, H.-Y., Yuan, Y.A. (2010). Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase. Journal of Molecular Cell Biology 2 (6) : 366-374. ScholarBank@NUS Repository. https://doi.org/10.1093/jmcb/mjq034|
|Abstract:||The proteins in DUF358 family are all bacterial proteins, which are ∼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 Á resolution. The structure reveals a single domain structure consisting of eight-stranded β-sheets sandwiched by six α-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 α-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. © The Author (2010).|
|Source Title:||Journal of Molecular Cell Biology|
|Appears in Collections:||Staff Publications|
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