2aly: Difference between revisions

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New page: left|200px<br /><applet load="2aly" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aly, resolution 2.60Å" /> '''Crystal Structure of...
 
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[[Image:2aly.gif|left|200px]]<br /><applet load="2aly" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2aly, resolution 2.60&Aring;" />
'''Crystal Structure of T.Thermophilus Phenylalanyl-tRNA synthetase complexed with 5'-O-[N-(L-tyrosyl)sulphamoyl]adenosine'''<br />


==Overview==
==Crystal Structure of T.Thermophilus Phenylalanyl-tRNA synthetase complexed with 5'-O-[N-(L-tyrosyl)sulphamoyl]adenosine==
Aminoacyl-tRNA synthetases (aaRSs) exert control over the faithful, transfer of amino acids onto cognate tRNAs. Since chemical structures of, various amino acids closely resemble each other, it is difficult to, discriminate between them. Editing activity has been evolved by certain, aaRSs to resolve the problem. In this study, we determined the crystal, structures of complexes of T. thermophilus phenylalanyl-tRNA synthetase, (PheRS) with L-tyrosine, p-chloro-phenylalanine, and a nonhydrolyzable, tyrosyl-adenylate analog. The structures demonstrate plasticity of the, synthetic site capable of binding substrates larger than phenylalanine and, provide a structural basis for the proofreading mechanism. The editing, site is localized at the B3/B4 interface, 35 A from the synthetic site., Glubeta334 plays a crucial role in the specific recognition of the Tyr, moiety in the editing site. The tyrosyl-adenylate analog binds exclusively, in the synthetic site. Both structural data and tyrosine-dependent ATP, hydrolysis enhanced by tRNA(Phe) provide evidence for a preferential, posttransfer editing pathway in the phenylalanine-specific system.
<StructureSection load='2aly' size='340' side='right'caption='[[2aly]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2aly]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ALY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ALY 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YSA:5-O-[N-(L-TYROSYL)SULFAMOYL]ADENOSINE'>YSA</scene></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=2aly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aly OCA], [https://pdbe.org/2aly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aly RCSB], [https://www.ebi.ac.uk/pdbsum/2aly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aly ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYFA_THETH SYFA_THETH]
== 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/al/2aly_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=2aly ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2ALY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with MN, SO4 and YSA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phenylalanine--tRNA_ligase Phenylalanine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.20 6.1.1.20] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ALY OCA].
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structural basis for discrimination of L-phenylalanine from L-tyrosine by phenylalanyl-tRNA synthetase., Kotik-Kogan O, Moor N, Tworowski D, Safro M, Structure. 2005 Dec;13(12):1799-807. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16338408 16338408]
[[Category: Large Structures]]
[[Category: Phenylalanine--tRNA ligase]]
[[Category: Thermus thermophilus HB8]]
[[Category: Protein complex]]
[[Category: Kotik-Kogan OM]]
[[Category: Thermus thermophilus]]
[[Category: Moor NA]]
[[Category: Kotik-Kogan, O.M.]]
[[Category: Safro MG]]
[[Category: Moor, N.A.]]
[[Category: Tworowski DE]]
[[Category: Safro, M.G.]]
[[Category: Tworowski, D.E.]]
[[Category: MN]]
[[Category: SO4]]
[[Category: YSA]]
[[Category: protein-ligand complex]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:12:51 2007''

Latest revision as of 12:13, 14 February 2024

Crystal Structure of T.Thermophilus Phenylalanyl-tRNA synthetase complexed with 5'-O-[N-(L-tyrosyl)sulphamoyl]adenosineCrystal Structure of T.Thermophilus Phenylalanyl-tRNA synthetase complexed with 5'-O-[N-(L-tyrosyl)sulphamoyl]adenosine

Structural highlights

2aly is a 2 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SYFA_THETH

Evolutionary Conservation

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

See Also

2aly, resolution 2.60Å

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OCA
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