1il2
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(New page: 200px<br /><applet load="1il2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1il2, resolution 2.60Å" /> '''Crystal Structure of...)
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Revision as of 15:21, 20 November 2007
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Crystal Structure of the E. coli Aspartyl-tRNA Synthetase:Yeast tRNAasp:aspartyl-Adenylate Complex
Overview
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.
About this Structure
1IL2 is a Protein complex structure of sequences from Escherichia coli and Saccharomyces cerevisiae with SO4 and AMO as ligands. Active as Aspartate--tRNA ligase, with EC number 6.1.1.12 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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