CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.1280.10
Functional Family Peptidylprolyl isomerase

Enzyme Information
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)

Haemophilus influenzae Rd KW20
TRNA (cytidine(34)-2'-O)-methyltransferase

PDB Structure

PDB 1J85
External Links
Organism Escherichia
Primary Citation
Structure of the YibK methyltransferase from Haemophilus influenzae (HI0766): A cofactor bound at a site formed by a knot
Lim, K., Zhang, H., Tempcyzk, A., Krajewski, W., Bonander, N., Toedt, J., Howard, A., Eisenstein, E., Herzberg, O.