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

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: 11566892
DOI: 10.1093/emboj/20.18.5290

Experimental method

X-RAY DIFFRACTION (2.6 Å)