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2aly

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[[Image:2aly.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of T.Thermophilus Phenylalanyl-tRNA synthetase complexed with 5'-O-[N-(L-tyrosyl)sulphamoyl]adenosine==
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|PDB= 2aly |SIZE=350|CAPTION= <scene name='initialview01'>2aly</scene>, resolution 2.60&Aring;
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<StructureSection load='2aly' size='340' side='right'caption='[[2aly]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=YSA:5'-O-[N-(L-TYROSYL)SULFAMOYL]ADENOSINE'>YSA</scene>
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<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>
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|ACTIVITY= [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]
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</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>
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|GENE=
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<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>
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}}
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYFA_THETH SYFA_THETH]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/al/2aly_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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'''Crystal Structure of T.Thermophilus Phenylalanyl-tRNA synthetase complexed with 5'-O-[N-(L-tyrosyl)sulphamoyl]adenosine'''
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==See Also==
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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[[Category: Thermus thermophilus HB8]]
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==About this Structure==
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[[Category: Kotik-Kogan OM]]
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2ALY is a [[Protein complex]] 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=2ALY OCA].
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[[Category: Moor NA]]
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[[Category: Safro MG]]
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==Reference==
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[[Category: Tworowski DE]]
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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://www.ncbi.nlm.nih.gov/pubmed/16338408 16338408]
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[[Category: Phenylalanine--tRNA ligase]]
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[[Category: Protein complex]]
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[[Category: Thermus thermophilus]]
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[[Category: Kotik-Kogan, O M.]]
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[[Category: Moor, N A.]]
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[[Category: Safro, M G.]]
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[[Category: Tworowski, D E.]]
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[[Category: MN]]
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[[Category: SO4]]
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[[Category: YSA]]
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[[Category: protein-ligand complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:51:10 2008''
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Current revision

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

PDB ID 2aly

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