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New page: left|200px<br /><applet load="1nyl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nyl, resolution 2.60Å" /> '''Unliganded glutaminy...
 
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[[Image:1nyl.jpg|left|200px]]<br /><applet load="1nyl" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1nyl, resolution 2.60&Aring;" />
'''Unliganded glutaminyl-tRNA synthetase'''<br />


==Overview==
==Unliganded glutaminyl-tRNA synthetase==
The crystal structure of ligand-free E. coli glutaminyl-tRNA synthetase, (GlnRS) at 2.4 A resolution shows that substrate binding is essential to, construction of a catalytically proficient active site. tRNA binding, generates structural changes throughout the enzyme, repositioning key, active site peptides that bind glutamine and ATP. The structure gives, insight into longstanding questions regarding the tRNA dependence of, glutaminyl adenylate formation, the coupling of amino acid and tRNA, selectivities, and the roles of specific pathways for transmission of tRNA, binding signals to the active site. Comparative analysis of the unliganded, and tRNA-bound structures shows, in detail, how flexibility is built into, the enzyme architecture and suggests that the induced-fit transitions are, a key underlying determinant of both amino acid and tRNA specificity.
<StructureSection load='1nyl' size='340' side='right'caption='[[1nyl]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1nyl]] is a 1 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=1NYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NYL 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]] 2.6&#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=1nyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nyl OCA], [https://pdbe.org/1nyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nyl RCSB], [https://www.ebi.ac.uk/pdbsum/1nyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nyl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYQ_ECOLI SYQ_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/ny/1nyl_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1nyl ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of ligand-free E. coli glutaminyl-tRNA synthetase (GlnRS) at 2.4 A resolution shows that substrate binding is essential to construction of a catalytically proficient active site. tRNA binding generates structural changes throughout the enzyme, repositioning key active site peptides that bind glutamine and ATP. The structure gives insight into longstanding questions regarding the tRNA dependence of glutaminyl adenylate formation, the coupling of amino acid and tRNA selectivities, and the roles of specific pathways for transmission of tRNA binding signals to the active site. Comparative analysis of the unliganded and tRNA-bound structures shows, in detail, how flexibility is built into the enzyme architecture and suggests that the induced-fit transitions are a key underlying determinant of both amino acid and tRNA specificity.


==About this Structure==
tRNA-dependent active site assembly in a class I aminoacyl-tRNA synthetase.,Sherlin LD, Perona JJ Structure. 2003 May;11(5):591-603. PMID:12737824<ref>PMID:12737824</ref>
1NYL 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/Glutamine--tRNA_ligase Glutamine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.18 6.1.1.18] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NYL OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
tRNA-dependent active site assembly in a class I aminoacyl-tRNA synthetase., Sherlin LD, Perona JJ, Structure. 2003 May;11(5):591-603. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12737824 12737824]
</div>
<div class="pdbe-citations 1nyl" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Glutamine--tRNA ligase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Perona JP]]
[[Category: Perona, J.P.]]
[[Category: Sherlin LD]]
[[Category: Sherlin, L.D.]]
[[Category: ligase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:39:49 2007''

Latest revision as of 00:18, 21 November 2024

Unliganded glutaminyl-tRNA synthetase

1nyl, resolution 2.60Å

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