1M83

Crystal Structure of Tryptophanyl-tRNA Synthetase Complexed with ATP in a Closed, Pre-transition State Conformation

Summary for 1M83

• Entry DOI: 10.2210/pdb1m83/pdb
• Related: 1D2R 1I6M
• Descriptor: Tryptophan-tRNA ligase, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: aminoacyl-trna synthetase, atp binding site, rossmann fold, ligase
• Biological source: Geobacillus stearothermophilus
• Cellular location: Cytoplasm: P00953
• Total number of polymer chains: 1
• Total formula weight: 38033.44

Authors

Retailleau, P.,Huang, X.,Yin, Y.,Hu, M.,Weinreb, V.,Vachette, P.,Vonrhein, C.,Bricogne, G.,Roversi, P.,Ilyin, V.,Carter Jr., C.W. (deposition date: 2002-07-24, release date: 2002-12-18, Last modification date: 2024-02-14)

• Primary citation: Retailleau, P.,Huang, X.,Yin, Y.,Hu, M.,Weinreb, V.,Vachette, P.,Vonrhein, C.,Bricogne, G.,Roversi, P.,Ilyin, V.,Carter, C.W.; Interconversion of ATP binding and conformational free energies by tryptophanyl-tRNA synthetase: structures of ATP bound to open and closed, pre-transition-state conformations.; J.Mol.Biol., 325:39-63, 2003; PubMed: 12473451; DOI: 10.1016/S0022-2836(02)01156-7

Experimental method

X-RAY DIFFRACTION (2.2 Å)