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Literature summary for 2.3.1.193 extracted from
- RNA helicase module in an acetyltransferase that modifies a specific tRNA anticodon (2009), EMBO J., 28, 1362-1373.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure of tRNAMet cytidine acetyltransferase from Escherichia coli complexed with two natural ligands, acetyl-CoA and ADP, at 2.35 A resolution. The structure reveals an idiosyncratic RNA helicase module fused with a GCN5-related N-acetyltransferase (GNAT) fold, which intimately crossinteract. It is proposed that an RNA helicase motor driven by ATP hydrolysis is used to deliver the wobble base to the active centre of the GNAT domain | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P76562 | - |
- |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | posttranscriptional RNA modifications in the anticodon of transfer RNAs contributes to the high fidelity of protein synthesis. In eubacteria, two genome-encoded tRNA species bear the same CAU sequence as the anticodons, which are differentiated by modified cytidines at the wobble positions. The elongator tRNAMet accepts an acetyl moiety at the wobble base to form N4-acetylcytidine (ac4C): an inherent modification ensures precise decoding of the AUG codon by strengthening C-G base-pair interaction and concurrently preventing misreading of the near cognate AUA codon | Escherichia coli |
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