Please use this identifier to cite or link to this item:
|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|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Jan 23, 2019
WEB OF SCIENCETM
checked on Jan 7, 2019
checked on Jan 18, 2019
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.