CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.1280 | Alpha/beta knot |
|
3.40.1280.10 | SPOUT methyltransferase, trefoil knot domain |
Domain Context
CATH Clusters
| Superfamily | 3.40.1280.10 |
| Functional Family | Peptidylprolyl isomerase |
Enzyme Information
| 2.1.1.207 |
tRNA (cytidine(34)-2'-O)-methyltransferase.
based on mapping to UniProt P44868
(1) S-adenosyl-L-methionine + cytidine(34) in tRNA = S-adenosyl-L- homocysteine + 2'-O-methylcytidine(34) in tRNA. (2) S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine(34) in tRNA(Leu) = S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O- methyluridine(34) in tRNA(Leu).
-!- The enzyme from Escherichia coli catalyzes the 2'-O-methylation of cytidine or 5-carboxymethylaminomethyluridine at the wobble position at nucleotide 34 in tRNA(Leu)CmAA and tRNA(Leu)cmnm(5)UmAA. -!- The enzyme is selective for the two tRNA(Leu) isoacceptors and only methylates these when they present the correct anticodon loop sequence and modification pattern. -!- Specifically, YibK requires a pyrimidine nucleoside at position 34, it has a clear preference for an adenosine at position 35, and it fails to methylate without prior addition of the N(6)-(isopentenyl)- 2-methylthioadenosine modification at position 37.
|
UniProtKB Entries (1)
| P44868 |
TRML_HAEIN
Haemophilus influenzae Rd KW20
TRNA (cytidine(34)-2'-O)-methyltransferase
|
PDB Structure
| PDB | 1MXI |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of the YibK methyltransferase from Haemophilus influenzae (HI0766): a Cofactor Bound at a Site Formed by a Knot
Proteins
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