2D6F

Crystal structure of Glu-tRNA(Gln) amidotransferase in the complex with tRNA(Gln)

Summary for 2D6F

• Entry DOI: 10.2210/pdb2d6f/pdb
• Descriptor: tRNA, Glutamyl-tRNA(Gln) amidotransferase subunit D, Glutamyl-tRNA(Gln) amidotransferase subunit E, ... (5 entities in total)
• Functional Keywords: ligase, rna, ligase-rna complex, ligase/rna
• Biological source: Methanothermobacter thermautotrophicus; More
• Total number of polymer chains: 6
• Total formula weight: 283160.20

Authors

Nureki, O. (deposition date: 2005-11-13, release date: 2006-07-11, Last modification date: 2024-03-13)

Primary citation

Oshikane, H.,Sheppard, K.,Fukai, S.,Nakamura, Y.,Ishitani, R.,Numata, T.,Sherrer, R.L.,Feng, L.,Schmitt, E.,Panvert, M.,Blanquet, S.,Mechulam, Y.,Soll, D.,Nureki, O.
Structural basis of RNA-dependent recruitment of glutamine to the genetic code
Science, 312:1950-1954, 2006

PubMed Abstract: Glutaminyl-transfer RNA (Gln-tRNA(Gln)) in archaea is synthesized in a pretranslational amidation of misacylated Glu-tRNA(Gln) by the heterodimeric Glu-tRNA(Gln) amidotransferase GatDE. Here we report the crystal structure of the Methanothermobacter thermautotrophicus GatDE complexed to tRNA(Gln) at 3.15 angstroms resolution. Biochemical analysis of GatDE and of tRNA(Gln) 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. tRNA(Gln) 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.

PubMed: 16809540
DOI: 10.1126/science.1128470

Experimental method

X-RAY DIFFRACTION (3.15 Å)