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 Q74Y93
(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)

Yersinia pestis
TRNA (cytidine(34)-2'-O)-methyltransferase

PDB Structure

External Links
Primary Citation
X-ray crystal structure of putative RNA methyltransferase from Yersinia pestis.
Osipiuk, J., Maltseva, N., Peterson, S., Anderson, W.F., Joachimiak, A.
To be Published