1QTQ

GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH TRNA AND AN AMINO ACID ANALOG

Summary for 1QTQ

Entry DOI	10.2210/pdb1qtq/pdb
Descriptor	RNA (TRNA GLN II ), PROTEIN (GLUTAMINYL-TRNA SYNTHETASE), SULFATE ION, ... (5 entities in total)
Functional Keywords	trna synthetase, glutamine, trnagln, e. coli, complex, ligase-rna complex, ligase/rna
Biological source	Escherichia coli More
Cellular location	Cytoplasm: P00962
Total number of polymer chains	2
Total formula weight	88353.63
Authors	Rath, V.L.,Silvian, L.F.,Beijer, B.,Sproat, B.S.,Steitz, T.A. (deposition date: 1998-01-28, release date: 1998-05-27, Last modification date: 2023-08-02)
Primary citation	Rath, V.L.,Silvian, L.F.,Beijer, B.,Sproat, B.S.,Steitz, T.A. How glutaminyl-tRNA synthetase selects glutamine. Structure, 6:439-449, 1998 Cited by PubMed Abstract: 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. PubMed: 9562563 DOI: 10.1016/S0969-2126(98)00046-X PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.25 Å)

Structure validation