Structural basis of RNA-dependent recruitment of glutamine to the genetic code

Hiroyuki Oshikane, Kelly Sheppard, Shuya Fukai, Yuko Nakamura, Ryuichiro Ishitani, Tomoyuki Numata, R. Lynn Sherrer, Liang Feng, Emmanuelle Schmitt, Michel Panvert, Sylvain Blanquet, Yves Mechulam, Dieter Söll, Osamu Nureki

Research output: Contribution to journalArticlepeer-review

77 Citations (Scopus)


Glutaminyl-transfer RNA (Gln-tRNAGln) in archaea is synthesized in a pretranslational amidation of misacylated Glu-tRNAGln by the heterodimeric Glu-tRNAGln amidotransferase GatDE. Here we report the crystal structure of the Methanothermobacter thermautotrophicus GatDE complexed to tRNAGln at 3.15 angstroms resolution. Biochemical analysis of GatDE and of tRNAGln mutants characterized the catalytic centers for the enzyme's three reactions (glutaminase, kinase, and amidotransferase activity). A 40 angstrom-long channel for ammonia transport connects the active sites in GatD and GatE. tRNAGln recognition by indirect readout based on shape complementarity of the D loop suggests an early antkodon-independent RNA-based mechanism for adding glutamine to the genetic code.

Original languageEnglish
Pages (from-to)1950-1954
Number of pages5
Issue number5782
Publication statusPublished - Jun 30 2006
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General


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