2ajg: Difference between revisions

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New page: left|200px<br /><applet load="2ajg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ajg, resolution 2.00Å" /> '''Crystal structure of...
 
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[[Image:2ajg.jpg|left|200px]]<br /><applet load="2ajg" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Crystal structure of the editing domain of E. coli leucyl-tRNA synthetase'''<br />


==Overview==
==Crystal structure of the editing domain of E. coli leucyl-tRNA synthetase==
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.
<StructureSection load='2ajg' size='340' side='right'caption='[[2ajg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYL_ECOLI SYL_ECOLI]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aj/2ajg_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2AJG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AJG OCA].
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16277600 16277600]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Leucine--tRNA ligase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Ding J]]
[[Category: Ding, J.]]
[[Category: Liao J]]
[[Category: Liao, J.]]
[[Category: Liu Y]]
[[Category: Liu, Y.]]
[[Category: Wang ED]]
[[Category: Wang, E.D.]]
[[Category: Zhu B]]
[[Category: Zhu, B.]]
[[Category: editing domain]]
[[Category: leucyl-trna synthetase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:10:05 2007''

Latest revision as of 16:41, 13 March 2024

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

Structural highlights

2ajg is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SYL_ECOLI

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2ajg, resolution 2.00Å

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OCA
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