Publications

• GLUTAMYL AND GLUTAMINYL RIBONUCLEIC ACID SYNTHETASES OF ESCHERICHIA COLI W. SEPARATION, PROPERTIES, AND STIMULATION OF ADENOSINE TRIPHOSPHATE-PYROPHOSPHATE EXCHANGE BY ACCEPTOR RIBONUCLEIC ACID.

  RAVEL J.M., WANG S.F., HEINEMEYER C., SHIVE W.

  J Biol Chem 240:432-438(1965) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• The structure of yeast glutaminyl-tRNA synthetase and modeling of its interaction with tRNA.

  Grant T.D., Luft J.R., Wolfley J.R., Snell M.E., Tsuruta H., Corretore S., Quartley E., Phizicky E.M., Grayhack E.J., Snell E.H.

  Eukaryotic glutaminyl-tRNA synthetase (GlnRS) contains an appended N-terminal domain (NTD) whose precise function is unknown. Although GlnRS structures from two prokaryotic species are known, no eukaryotic GlnRS structure has been reported. Here we present the first crystallographic structure of y ... >> More

  Eukaryotic glutaminyl-tRNA synthetase (GlnRS) contains an appended N-terminal domain (NTD) whose precise function is unknown. Although GlnRS structures from two prokaryotic species are known, no eukaryotic GlnRS structure has been reported. Here we present the first crystallographic structure of yeast GlnRS, finding that the structure of the C-terminal domain is highly similar to Escherichia coli GlnRS but that 214 residues, including the NTD, are crystallographically disordered. We present a model of the full-length enzyme in solution, using the structures of the C-terminal domain, and the isolated NTD, with small-angle X-ray scattering data of the full-length molecule. We proceed to model the enzyme bound to tRNA, using the crystallographic structures of GatCAB and GlnRS-tRNA complex from bacteria. We contrast the tRNA-bound model with the tRNA-free solution state and perform molecular dynamics on the full-length GlnRS-tRNA complex, which suggests that tRNA binding involves the motion of a conserved hinge in the NTD. << Less

  J Mol Biol 425:2480-2493(2013) [PubMed] [EuropePMC]

• How glutaminyl-tRNA synthetase selects glutamine.

  Rath V.L., Silvian L.F., Beijer B., Sproat B.S., Steitz T.A.

  <h4>Background</h4>Aminoacyl-tRNA synthetases covalently link a specific amino acid to the correct tRNA. The fidelity of this reaction is essential for accurate protein synthesis. Each synthetase has a specific molecular mechanism to distinguish the correct pair of substrates from the pool of amin ... >> More

  <h4>Background</h4>Aminoacyl-tRNA synthetases covalently link a specific amino acid to the correct tRNA. The fidelity of this reaction is essential for accurate protein synthesis. Each synthetase has a specific molecular mechanism to distinguish the correct pair of substrates from the pool of amino acids and isologous tRNA molecules. In the case of glutaminyl-tRNA synthetase (GlnRS) the prior binding of tRNA is required for activation of glutamine by ATP. A complete understanding of amino acid specificity in GlnRS requires the determination of the structure of the synthetase with both tRNA and substrates bound.<h4>Results</h4>A stable glutaminly-adenylate analog, which inhibits GlnRS with a Ki of 1.32 microM, was synthesized and cocrystallized with GlnRS and tRNA2Gln. The crystal structure of this ternary complex has been refined at 2.4 A resolution and shows the interactions made between glutamine and its binding site.<h4>Conclusions</h4>To select against glutamic acid or glutamate, both hydrogen atoms of the nitrogen of the glutamine sidechain are recognized. The hydroxyl group of Tyr211 and a water molecule are responsible for this recognition; both are obligate hydrogen-bond acceptors due to a network of interacting sidechains and water molecules. The prior binding of tRNAGln that is required for amino acid activation may result from the terminal nucleotide, A76, packing against and orienting Tyr211, which forms part of the amino acid binding site. << Less

  Structure 6:439-449(1998) [PubMed] [EuropePMC]