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1IL2

Crystal Structure of the E. coli Aspartyl-tRNA Synthetase:Yeast tRNAasp:aspartyl-Adenylate Complex

Summary for 1IL2
Entry DOI10.2210/pdb1il2/pdb
DescriptorASPARTYL TRANSFER RNA, ASPARTYL-TRNA SYNTHETASE, SULFATE ION, ... (5 entities in total)
Functional Keywordsprotein-rna complex, ligase-rna complex, ligase/rna
Biological sourceEscherichia coli
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Cellular locationCytoplasm: P21889
Total number of polymer chains4
Total formula weight181472.11
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 citationMoulinier, 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: 11566892
DOI: 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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