Literature summary extracted from
Chen, H.; Yuan, Y.
Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase (2010), J. Mol. Cell Biol., 2, 366-374.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.1.1.257 |
gene Mj1640, expression of wild-type and selenmethionine-labeled enzyme as N-terminally His-tagged protein in Escherichia coli strain Bl21(DE3) |
Methanocaldococcus jannaschii |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.1.1.257 |
purified recombinant wild-type and selenmethionine-labeled DUF358/Mj1640 in complex with S-adenosyl-L-methionine, at 20°C, mixing of 0.001 ml of protein solution with 0.001 l of reservoir containing 20% PEG 3350, 25 mM NH4F, 20 mM MgCl2, 100 mM Tris, pH 7.5, X-ray diffraction structure determination and analysis at 1.4 A resolution |
Methanocaldococcus jannaschii |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.1.1.257 |
Methanocaldococcus jannaschii |
Q59034 |
gene Mj1640 |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.1.1.257 |
recombinant His-tagged wild-type and selenmethionine-labeled Mj1640 from Escherichia coli strain Bl21(DE3) by nickel affinity chromatography and gel filtration |
Methanocaldococcus jannaschii |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.1.1.257 |
additional information |
SAM-binding pocket Asp157 or Glu183 from its own monomer or Ser43 from the associate monomer probably plays the catalytic role for RNA methylation, RNA-binding residues and putative active site, overview |
Methanocaldococcus jannaschii |
? |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.1.1.257 |
dimer |
Mj1640 forms a dimer, which is mediated by two parallel pairs of alpha-helices oriented almost perpendicular to each other |
Methanocaldococcus jannaschii |
2.1.1.257 |
More |
the enzyme shows a single domain structure consisting of eight-stranded beta-sheets sandwiched by six alpha-helices at both sides. Mj1640 has limited structural extension at its N-terminus, which is unique to this family member, structure modeling based on the crystal structure, overview |
Methanocaldococcus jannaschii |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.1.1.257 |
DUF358/Mj1640 |
- |
Methanocaldococcus jannaschii |
2.1.1.257 |
m1-pseudouridine methyltransferase |
- |
Methanocaldococcus jannaschii |
2.1.1.257 |
m1G |
- |
Methanocaldococcus jannaschii |
2.1.1.257 |
M3U |
- |
Methanocaldococcus jannaschii |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.1.1.257 |
evolution |
the enzyme is a SPOUT-class RNA methyltransferase and belongs to the DUF358 family. The DUF358/Mj1640 protein shows close structural relationship to Nep1, a pseudouridine-N1-specific rRNA methyltransferase |
Methanocaldococcus jannaschii |