Summary information and primary citation
- PDB-id
-
1il2;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- ligase-RNA
- Method
- X-ray (2.6 Å)
- Summary
- Crystal structure of the e. coli aspartyl-trna
synthetase:yeast trnaasp:aspartyl-adenylate complex
- Reference
-
Moulinier L, Eiler S, Eriani G, Gangloff J, Thierry JC,
Gabriel K, McClain WH, Moras D (2001): "The
structure of an AspRS-tRNA(Asp) complex reveals a
tRNA-dependent control mechanism." EMBO J.,
20, 5290-5301. doi: 10.1093/emboj/20.18.5290.
- 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.
