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Literature summary for 2.8.1.13 extracted from

  • Numata, T.; Ikeuchi, Y.; Fukai, S.; Suzuki, T.; Nureki, O.
    Snapshots of tRNA sulphuration via an adenylated intermediate (2006), Nature, 442, 419-424.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of the MnmA thiouridylase–tRNA(Glu) binary complex in three discrete forms, which provide snapshots of the sequential chemical reactions during RNA sulfuration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P25745
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-

Reaction

Reaction Comment Organism Reaction ID
a [protein]-S-sulfanyl-L-cysteine + uacil34 in tRNA + ATP + reduced acceptor = a [protein]-L-cysteine + 2-thiouracil34 in tRNA + AMP + diphosphate + acceptor on enzyme activation, an alpha-helix overhanging the active site is restructured into an idiosyncratic beta-hairpin-containing loop, which packs the flipped-out U34 deeply into the catalytic pocket and triggers the activation of the catalytic cysteine residues. The adenylated RNA intermediate is trapped. The active closed-conformation of the complex ensures accurate sulfur incorporation into the activated uridine carbon by forming a catalytic chamber to prevent solvent from accessing the catalytic site Escherichia coli

Synonyms

Synonyms Comment Organism
MnmA
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Escherichia coli