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2ajg

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[[Image:2ajg.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of the editing domain of E. coli leucyl-tRNA synthetase==
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|PDB= 2ajg |SIZE=350|CAPTION= <scene name='initialview01'>2ajg</scene>, resolution 2.00&Aring;
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<StructureSection load='2ajg' size='340' side='right'caption='[[2ajg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2ajg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AJG FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Leucine--tRNA_ligase Leucine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.4 6.1.1.4] </span>
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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&#8491;</td></tr>
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|GENE=
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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=2ajg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajg OCA], [https://pdbe.org/2ajg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ajg RCSB], [https://www.ebi.ac.uk/pdbsum/2ajg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ajg ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[2ajh|2AJH]], [[2aji|2AJI]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ajg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajg OCA], [http://www.ebi.ac.uk/pdbsum/2ajg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ajg RCSB]</span>
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[https://www.uniprot.org/uniprot/SYL_ECOLI SYL_ECOLI]
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}}
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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/aj/2ajg_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=2ajg ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of the editing domain of E. coli leucyl-tRNA synthetase'''
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==See Also==
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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aaRSs (aminoacyl-tRNA synthetases) are responsible for the covalent linking of amino acids to their cognate tRNAs via the aminoacylation reaction and play a vital role in maintaining the fidelity of protein synthesis. LeuRS (leucyl-tRNA synthetase) can link not only the cognate leucine but also the nearly cognate residues Ile and Met to tRNA(Leu). The editing domain of LeuRS deacylates the mischarged Ile-tRNA(Leu) and Met-tRNA(Leu). We report here the crystal structures of ecLeuRS-ED (the editing domain of Escherichia coli LeuRS) in both the apo form and in complexes with Met and Ile at 2.0 A, 2.4 A, and 3.2 A resolution respectively. The editing active site consists of a number of conserved amino acids, which are involved in the precise recognition and binding of the noncognate amino acids. The substrate-binding pocket has a rigid structure which has an optimal stereochemical fit for Ile and Met, but has steric hindrance for leucine. Based on our structural results and previously available biochemical data, we propose that ecLeuRS-ED uses a lock-and-key mechanism to recognize and discriminate between the amino acids. Structural comparison also reveals that all subclass Ia aaRSs share a conserved structure core consisting of the editing domain and conserved residues at the editing active site, suggesting that these enzymes may use a common mechanism for the editing function.
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==About this Structure==
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2AJG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJG OCA].
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==Reference==
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Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination., Liu Y, Liao J, Zhu B, Wang ED, Ding J, Biochem J. 2006 Mar 1;394(Pt 2):399-407. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16277600 16277600]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Leucine--tRNA ligase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Ding J]]
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[[Category: Ding, J.]]
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[[Category: Liao J]]
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[[Category: Liao, J.]]
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[[Category: Liu Y]]
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[[Category: Liu, Y.]]
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[[Category: Wang ED]]
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[[Category: Wang, E D.]]
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[[Category: Zhu B]]
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[[Category: Zhu, B.]]
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[[Category: editing domain]]
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[[Category: leucyl-trna synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:53:30 2008''
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Current revision

Crystal structure of the editing domain of E. coli leucyl-tRNA synthetase

PDB ID 2ajg

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