1il2

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{{STRUCTURE_1il2| PDB=1il2 | SCENE= }}
{{STRUCTURE_1il2| PDB=1il2 | SCENE= }}
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'''Crystal Structure of the E. coli Aspartyl-tRNA Synthetase:Yeast tRNAasp:aspartyl-Adenylate Complex'''
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===Crystal Structure of the E. coli Aspartyl-tRNA Synthetase:Yeast tRNAasp:aspartyl-Adenylate Complex===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11566892 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11566892}}
==About this Structure==
==About this Structure==
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[[Category: Thierry, J C.]]
[[Category: Thierry, J C.]]
[[Category: Protein-rna complex]]
[[Category: Protein-rna complex]]
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Revision as of 10:26, 1 July 2008

Template:STRUCTURE 1il2

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

Template:ABSTRACT PUBMED 11566892

About this Structure

1IL2 is a Protein complex structure of sequences from Escherichia coli and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism., Moulinier L, Eiler S, Eriani G, Gangloff J, Thierry JC, Gabriel K, McClain WH, Moras D, EMBO J. 2001 Sep 17;20(18):5290-301. PMID:11566892

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