1il2: Difference between revisions
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[[Image:1il2.gif|left|200px]] | [[Image:1il2.gif|left|200px]] | ||
'''Crystal Structure of the E. coli Aspartyl-tRNA Synthetase:Yeast tRNAasp:aspartyl-Adenylate Complex''' | {{Structure | ||
|PDB= 1il2 |SIZE=350|CAPTION= <scene name='initialview01'>1il2</scene>, resolution 2.60Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=AMO:ASPARTYL-ADENOSINE-5'-MONOPHOSPHATE'>AMO</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''Crystal Structure of the E. coli Aspartyl-tRNA Synthetase:Yeast tRNAasp:aspartyl-Adenylate Complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1IL2 is a [ | 1IL2 is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IL2 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11566892 11566892] | ||
[[Category: Aspartate--tRNA ligase]] | [[Category: Aspartate--tRNA ligase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: protein-rna complex]] | [[Category: protein-rna complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:51:45 2008'' | ||
Revision as of 12:51, 20 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Aspartate--tRNA ligase, with EC number 6.1.1.12 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the E. coli Aspartyl-tRNA Synthetase:Yeast tRNAasp:aspartyl-Adenylate Complex
OverviewOverview
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 StructureAbout this Structure
1IL2 is a Protein complex structure of sequences from Escherichia coli and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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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