2ajh: Difference between revisions

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[[Image:2ajh.gif|left|200px]]


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==Crystal structure of the editing domain of E. coli leucyl-tRNA synthetase complexes with methionine==
The line below this paragraph, containing "STRUCTURE_2ajh", creates the "Structure Box" on the page.
<StructureSection load='2ajh' size='340' side='right'caption='[[2ajh]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2ajh]] 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=2AJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AJH FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#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=MET:METHIONINE'>MET</scene></td></tr>
{{STRUCTURE_2ajh|  PDB=2ajh |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ajh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajh OCA], [https://pdbe.org/2ajh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ajh RCSB], [https://www.ebi.ac.uk/pdbsum/2ajh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ajh 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/2ajh_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=2ajh ConSurf].
<div style="clear:both"></div>


'''Crystal structure of the editing domain of E. coli leucyl-tRNA synthetase complexes with methionine'''
==See Also==
 
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
 
==About this Structure==
2AJH 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=2AJH OCA].
 
==Reference==
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]
[[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://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:07:43 2008''

Latest revision as of 16:41, 13 March 2024

Crystal structure of the editing domain of E. coli leucyl-tRNA synthetase complexes with methionineCrystal structure of the editing domain of E. coli leucyl-tRNA synthetase complexes with methionine

Structural highlights

2ajh 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 2.4Å
Ligands:
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

2ajh, resolution 2.40Å

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