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Science 30 June 2006:
Vol. 312. no. 5782, pp. 1950 - 1954
DOI: 10.1126/science.1128470
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Reports
Structural Basis of RNA-Dependent Recruitment of Glutamine to the Genetic Code
Hiroyuki Oshikane,1*
Kelly Sheppard,2*
Shuya Fukai,1
Yuko Nakamura,1
Ryuichiro Ishitani,1
Tomoyuki Numata,1
R. Lynn Sherrer,2
Liang Feng,2
Emmanuelle Schmitt,3
Michel Panvert,3
Sylvain Blanquet,3
Yves Mechulam,3
Dieter Söll,2
Osamu Nureki1
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 anticodon-independent RNA-based mechanism for adding glutamine to the genetic code.
1 Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama-shi, Kanagawa 226-8501, Japan.
2 Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520–8114, USA.
3 Laboratoire de Biochimie, Unité Mixte de Recherche 7654, CNRS-Ecole Polytechnique, F-91128 Palaiseau Cedex, France.
* These authors contributed equally to this work.
 To whom correspondence should be addressed. E-mail: onureki{at}bio.titech.ac.jp (O.N.); dieter.soll{at}yale.edu (D.S.)
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