1il2
From Proteopedia
(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...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1il2.gif|left|200px]]<br /><applet load="1il2" size=" | + | [[Image:1il2.gif|left|200px]]<br /><applet load="1il2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1il2, resolution 2.60Å" /> | caption="1il2, resolution 2.60Å" /> | ||
'''Crystal Structure of the E. coli Aspartyl-tRNA Synthetase:Yeast tRNAasp:aspartyl-Adenylate Complex'''<br /> | '''Crystal Structure of the E. coli Aspartyl-tRNA Synthetase:Yeast tRNAasp:aspartyl-Adenylate Complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 2.6 A resolution crystal structure of an inactive complex between | + | 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== | ==About this Structure== | ||
| - | 1IL2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 and AMO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate--tRNA_ligase Aspartate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.12 6.1.1.12] Full crystallographic information is available from [http:// | + | 1IL2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=AMO:'>AMO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate--tRNA_ligase Aspartate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.12 6.1.1.12] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IL2 OCA]. |
==Reference== | ==Reference== | ||
| Line 19: | Line 19: | ||
[[Category: Gabriel, K.]] | [[Category: Gabriel, K.]] | ||
[[Category: Gangloff, J.]] | [[Category: Gangloff, J.]] | ||
| - | [[Category: McClain, W | + | [[Category: McClain, W H.]] |
[[Category: Moras, D.]] | [[Category: Moras, D.]] | ||
[[Category: Moulinier, L.]] | [[Category: Moulinier, L.]] | ||
| - | [[Category: Thierry, J | + | [[Category: Thierry, J C.]] |
[[Category: AMO]] | [[Category: AMO]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: protein-rna complex]] | [[Category: protein-rna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:57 2008'' |
Revision as of 11:12, 21 February 2008
|
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 and 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
Page seeded by OCA on Thu Feb 21 13:12:57 2008
