2cv2: Difference between revisions

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[[Image:2cv2.png|left|200px]]


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==Glutamyl-tRNA synthetase from Thermus thermophilus in complex with tRNA(Glu) and an enzyme inhibitor, Glu-AMS==
The line below this paragraph, containing "STRUCTURE_2cv2", creates the "Structure Box" on the page.
<StructureSection load='2cv2' size='340' side='right'caption='[[2cv2]], [[Resolution|resolution]] 2.69&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'>[[2cv2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CV2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CV2 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]] 2.69&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GSU:O5-(L-GLUTAMYL-SULFAMOYL)-ADENOSINE'>GSU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
{{STRUCTURE_2cv2| PDB=2cv2 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cv2 OCA], [https://pdbe.org/2cv2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cv2 RCSB], [https://www.ebi.ac.uk/pdbsum/2cv2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cv2 ProSAT], [https://www.topsan.org/Proteins/RSGI/2cv2 TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYE_THET8 SYE_THET8] Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).<ref>PMID:11224561</ref> <ref>PMID:17161369</ref>
== 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/cv/2cv2_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=2cv2 ConSurf].
<div style="clear:both"></div>


===Glutamyl-tRNA synthetase from Thermus thermophilus in complex with tRNA(Glu) and an enzyme inhibitor, Glu-AMS===
==See Also==
 
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 
*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
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== References ==
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<references/>
(as it appears on PubMed at http://www.pubmed.gov), where 17161369 is the PubMed ID number.
__TOC__
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</StructureSection>
{{ABSTRACT_PUBMED_17161369}}
[[Category: Large Structures]]
 
==About this Structure==
2CV2 is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CV2 OCA].
 
==Reference==
Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase., Sekine S, Shichiri M, Bernier S, Chenevert R, Lapointe J, Yokoyama S, Structure. 2006 Dec;14(12):1791-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17161369 17161369]
[[Category: Glutamate--tRNA ligase]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Sekine S]]
[[Category: Sekine, S.]]
[[Category: Yokoyama S]]
[[Category: Yokoyama, S.]]
[[Category: Ligase]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Riken structural genomics/proteomics initiative]]
[[Category: Rna]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Nov 16 16:40:44 2008''

Latest revision as of 16:43, 13 March 2024

Glutamyl-tRNA synthetase from Thermus thermophilus in complex with tRNA(Glu) and an enzyme inhibitor, Glu-AMSGlutamyl-tRNA synthetase from Thermus thermophilus in complex with tRNA(Glu) and an enzyme inhibitor, Glu-AMS

Structural highlights

2cv2 is a 4 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.69Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

SYE_THET8 Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).[1] [2]

Evolutionary Conservation

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

See Also

References

  1. ↑ Sekine S, Nureki O, Shimada A, Vassylyev DG, Yokoyama S. Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase. Nat Struct Biol. 2001 Mar;8(3):203-6. PMID:11224561 doi:10.1038/84927
  2. ↑ Sekine S, Shichiri M, Bernier S, Chenevert R, Lapointe J, Yokoyama S. Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase. Structure. 2006 Dec;14(12):1791-9. PMID:17161369 doi:10.1016/j.str.2006.10.005

2cv2, resolution 2.69Å

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