1IL2
Crystal Structure of the E. coli Aspartyl-tRNA Synthetase:Yeast tRNAasp:aspartyl-Adenylate Complex
Summary for 1IL2
Entry DOI | 10.2210/pdb1il2/pdb |
Descriptor | ASPARTYL TRANSFER RNA, ASPARTYL-TRNA SYNTHETASE, SULFATE ION, ... (5 entities in total) |
Functional Keywords | protein-rna complex, ligase-rna complex, ligase/rna |
Biological source | Escherichia coli More |
Cellular location | Cytoplasm: P21889 |
Total number of polymer chains | 4 |
Total formula weight | 181472.11 |
Authors | Moulinier, L.,Eiler, S.,Eriani, G.,Gangloff, J.,Thierry, J.C.,Gabriel, K.,McClain, W.H.,Moras, D. (deposition date: 2001-05-07, release date: 2001-09-28, Last modification date: 2024-04-03) |
Primary citation | Moulinier, L.,Eiler, S.,Eriani, G.,Gangloff, J.,Thierry, J.C.,Gabriel, K.,McClain, W.H.,Moras, D. The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism. EMBO J., 20:5290-5301, 2001 Cited by PubMed Abstract: The 2.6 A resolution crystal structure of an inactive complex between yeast tRNA(Asp) and Escherichia coli aspartyl-tRNA synthetase reveals the molecular details of a tRNA-induced mechanism that controls the specificity of the reaction. The dimer is asymmetric, with only one of the two bound tRNAs entering the active site cleft of its subunit. However, the flipping loop, which controls the proper positioning of the amino acid substrate, acts as a lid and prevents the correct positioning of the terminal adenosine. The structure suggests that the acceptor stem regulates the loop movement through sugar phosphate backbone- protein interactions. Solution and cellular studies on mutant tRNAs confirm the crucial role of the tRNA three-dimensional structure versus a specific recognition of bases in the control mechanism. PubMed: 11566892DOI: 10.1093/emboj/20.18.5290 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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