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Literature summary for 2.1.1.257 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.
    View publication on PubMed
Search for more literature for 2.1.1.257

Cloned(Commentary)

Cloned (Comment) Organism
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)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q59034 gene Mj1640
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Purification (Commentary)

Purification (Comment) Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
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 ?

Subunits

Subunits Comment Organism
dimer Mj1640 forms a dimer, which is mediated by two parallel pairs of alpha-helices oriented almost perpendicular to each other Methanocaldococcus jannaschii
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

Synonyms Comment Organism
DUF358/Mj1640
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 Methanocaldococcus jannaschii
m1-pseudouridine methyltransferase
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 Methanocaldococcus jannaschii
m1G
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 Methanocaldococcus jannaschii
M3U
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 Methanocaldococcus jannaschii

General Information

General Information Comment Organism
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