Ontology highlight
ABSTRACT:
SUBMITTER: Scrima A
PROVIDER: S-EPMC544919 | biostudies-literature | 2005 Jan
REPOSITORIES: biostudies-literature
Scrima Andrea A Vetter Ingrid R IR Armengod M Eugenia ME Wittinghofer Alfred A
The EMBO journal 20041216 1
TrmE is a 50 kDa guanine nucleotide-binding protein conserved between bacteria and man. It is involved in the modification of uridine bases (U34) at the first anticodon (wobble) position of tRNAs decoding two-family box triplets. The precise role of TrmE in the modification reaction is hitherto unknown. Here, we report the X-ray structure of TrmE from Thermotoga maritima. The structure reveals a three-domain protein comprising the N-terminal alpha/beta domain, the central helical domain and the ...[more]