1FL8

HYPERMODIFIED NUCLEOSIDES IN THE ANTICODON OF TRNALYS STABILIZE A CANONICAL U-TURN STRUCTURE

Summary for 1FL8

• Entry DOI: 10.2210/pdb1fl8/pdb
• Related: 1BZ2 1BZU
• Descriptor: ANTICODON DOMAIN OF TRNA(LYS) (1 entity in total)
• Functional Keywords: trna, anticodon, pseudouridine, mnm5s2u, t6a, rna
• Total number of polymer chains: 1
• Total formula weight: 5554.44

Authors

Sundaram, M.,Durant, P.C.,Davis, D.R. (deposition date: 2000-08-11, release date: 2000-10-16, Last modification date: 2024-05-22)

Primary citation

Sundaram, M.,Durant, P.C.,Davis, D.R.
Hypermodified nucleosides in the anticodon of tRNALys stabilize a canonical U-turn structure.
Biochemistry, 39:12575-12584, 2000

PubMed 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.

PubMed: 11027137
DOI: 10.1021/bi0014655

Experimental method

SOLUTION NMR