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 2.60&Aring;" /> '''Crystal Structure of...)
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[[Image:1il2.gif|left|200px]]<br /><applet load="1il2" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1il2, resolution 2.60&Aring;" />
 
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'''Crystal Structure of the E. coli Aspartyl-tRNA Synthetase:Yeast tRNAasp:aspartyl-Adenylate Complex'''<br />
 
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==Overview==
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==Crystal Structure of the E. coli Aspartyl-tRNA Synthetase:Yeast tRNAasp:aspartyl-Adenylate Complex==
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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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<StructureSection load='1il2' size='340' side='right'caption='[[1il2]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1il2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IL2 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1MG:1N-METHYLGUANOSINE-5-MONOPHOSPHATE'>1MG</scene>, <scene name='pdbligand=5MC:5-METHYLCYTIDINE-5-MONOPHOSPHATE'>5MC</scene>, <scene name='pdbligand=5MU:5-METHYLURIDINE+5-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=AMO:ASPARTYL-ADENOSINE-5-MONOPHOSPHATE'>AMO</scene>, <scene name='pdbligand=H2U:5,6-DIHYDROURIDINE-5-MONOPHOSPHATE'>H2U</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1il2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1il2 OCA], [https://pdbe.org/1il2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1il2 RCSB], [https://www.ebi.ac.uk/pdbsum/1il2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1il2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYD_ECOLI SYD_ECOLI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/il/1il2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1il2 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IL2 OCA].
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
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==Reference==
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__TOC__
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11566892 11566892]
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</StructureSection>
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[[Category: Aspartate--tRNA ligase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Eiler, S.]]
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[[Category: Eiler S]]
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[[Category: Eriani, G.]]
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[[Category: Eriani G]]
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[[Category: Gabriel, K.]]
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[[Category: Gabriel K]]
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[[Category: Gangloff, J.]]
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[[Category: Gangloff J]]
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[[Category: McClain, W.H.]]
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[[Category: McClain WH]]
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[[Category: Moras, D.]]
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[[Category: Moras D]]
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[[Category: Moulinier, L.]]
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[[Category: Moulinier L]]
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[[Category: Thierry, J.C.]]
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[[Category: Thierry JC]]
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[[Category: AMO]]
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[[Category: SO4]]
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[[Category: protein-rna complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:28:51 2007''
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Current revision

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

PDB ID 1il2

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