Summary information and primary citation
- PDB-id
-
1j2b;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- transferase-RNA
- Method
- X-ray (3.3 Å)
- Summary
- Crystal structure of archaeosine trna-guanine
transglycosylase complexed with lambda-form trna(val)
- Reference
-
Ishitani R, Nureki O, Nameki N, Okada N, Nishimura S,
Yokoyama S (2003): "Alternative
Tertiary Structure of tRNA for Recognition by a
Posttranscriptional Modification Enzyme."
Cell(Cambridge,Mass.), 113,
383-394. doi: 10.1016/S0092-8674(03)00280-0.
- Abstract
- Transfer RNA (tRNA) canonically has the clover-leaf
secondary structure with the acceptor, D, anticodon, and T
arms, which are folded into the L-shaped tertiary
structure. To strengthen the L form, posttranscriptional
modifications occur on nucleotides buried within the core,
but the modification enzymes are paradoxically inaccessible
to them in the L form. In this study, we determined the
crystal structure of tRNA bound with archaeosine
tRNA-guanine transglycosylase, which modifies G15 of the D
arm in the core. The bound tRNA assumes an alternative
conformation ("lambda form") drastically different from the
L form. All of the D-arm secondary base pairs and the
canonical tertiary interactions are disrupted. Furthermore,
a helical structure is reorganized, while the rest of the D
arm is single stranded and protruded. Consequently, the
enzyme precisely locates the exposed G15 in the active
site, by counting the nucleotide number from G1 to G15 in
the lambda form.