1il2

[[Image:1il2.gif|left|200px]]

{{Structure

|PDB= 1il2 |SIZE=350|CAPTION= <scene name='initialview01'>1il2</scene>, resolution 2.60&Aring;

|SITE=

|LIGAND= <scene name='pdbligand=1MG:1N-METHYLGUANOSINE-5&#39;-MONOPHOSPHATE'>1MG</scene>, <scene name='pdbligand=5MC:5-METHYLCYTIDINE-5&#39;-MONOPHOSPHATE'>5MC</scene>, <scene name='pdbligand=5MU:5-METHYLURIDINE+5&#39;-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=AMO:ASPARTYL-ADENOSINE-5&#39;-MONOPHOSPHATE'>AMO</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=H2U:5,6-DIHYDROURIDINE-5&#39;-MONOPHOSPHATE'>H2U</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5&#39;-MONOPHOSPHATE'>PSU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>

|ACTIVITY= <span class='plainlinks'>[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] </span>

|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1il2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1il2 OCA], [http://www.ebi.ac.uk/pdbsum/1il2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1il2 RCSB]</span>

 

 

==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.

 

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].

 

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: Protein complex]]

[[Category: Eiler, S.]]

[[Category: Eriani, G.]]

[[Category: Gabriel, K.]]

[[Category: Gangloff, J.]]

[[Category: McClain, W H.]]

[[Category: Moras, D.]]

[[Category: Moulinier, L.]]

[[Category: Thierry, J C.]]