Unknown

Dataset Information

0

The structure of the TrmE GTP-binding protein and its implications for tRNA modification.


ABSTRACT: 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 G domain, responsible for GTP binding and hydrolysis. The N-terminal domain induces dimerization and is homologous to the tetrahydrofolate-binding domain of N,N-dimethylglycine oxidase. Biochemical and structural studies show that TrmE indeed binds formyl-tetrahydrofolate. A cysteine residue, necessary for modification of U34, is located close to the C1-group donor 5-formyl-tetrahydrofolate, suggesting a direct role of TrmE in the modification analogous to DNA modification enzymes. We propose a reaction mechanism whereby TrmE actively participates in the formylation reaction of uridine and regulates the ensuing hydrogenation reaction of a Schiff's base intermediate.

SUBMITTER: Scrima A 

PROVIDER: S-EPMC544919 | biostudies-literature | 2005 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

The structure of the TrmE GTP-binding protein and its implications for tRNA modification.

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]

Similar Datasets

| S-EPMC2593442 | biostudies-literature
| S-EPMC2593692 | biostudies-literature
| S-EPMC135671 | biostudies-literature
| S-EPMC305853 | biostudies-literature
| S-EPMC8034428 | biostudies-literature
| S-EPMC6697224 | biostudies-literature
| S-EPMC3045595 | biostudies-literature
| S-EPMC164861 | biostudies-literature
| S-EPMC7888581 | biostudies-literature
| S-EPMC2757647 | biostudies-literature