Summary information and primary citation
- PDB-id
-
1fl8;
DSSR-derived features in text and
JSON formats
- Class
- RNA
- Method
- NMR
- Summary
- Hypermodified nucleosides in the anticodon of trnalys
stabilize a canonical u-turn structure
- Reference
-
Sundaram M, Durant PC, Davis DR (2000): "Hypermodified
nucleosides in the anticodon of tRNALys stabilize a
canonical U-turn structure." Biochemistry,
39, 12575-12584. doi: 10.1021/bi0014655.
- Abstract
- Modified nucleosides in the anticodon domain of
Escherichia coli tRNA(Lys) are necessary for high-affinity
codon recognition and reading frame maintenance. Human
tRNA(Lys,3) is the specific primer for HIV-1 reverse
transcriptase and also requires nucleoside modification for
proper function. We now present NMR solution structures for
the fully modified 17-nucleotide E. coli tRNA(Lys)
anticodon stem-loop domain (ASL). NMR data were also
collected for several partially modified ASLs, revealing
the contributions each modified nucleoside (mnm(5)s(2)U34,
t(6)A37, and psi39) makes in transforming the disordered,
unmodified tRNA ASL into the highly ordered native
structure. The solution structure of the native ASL domain
provides insight into longstanding questions regarding both
wobble position modification and the nearly ubiquitous
t(6)A37 found in tRNAs with an adjacent U at position 36.
Native tRNA(Lys) has a U-turn structure similar to the
yeast tRNA(Phe) crystal structure, unlike previously
proposed "unconventional" anticodon structures
characterized by stable interactions between mnm(5)s(2)U-34
and t(6)A-37.
