ArcTGT-tRNA complex
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.
![1J2B-1.png 1J2B-1.png](http://nurekilab.net/index.php/ja?plugin=ref&page=Gallery%2FRNA%2F1J2B&src=1J2B-1.png) |
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.
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![1J2B-2.png 1J2B-2.png](http://nurekilab.net/index.php/ja?plugin=ref&page=Gallery%2FRNA%2F1J2B&src=1J2B-2.png) |
The bound tRNA assumes an alternative conformation ("λ 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.
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![1J2B-3.png 1J2B-3.png](http://nurekilab.net/index.php/ja?plugin=ref&page=Gallery%2FRNA%2F1J2B&src=1J2B-3.png) |
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.
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