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<StructureSection load='1pys' size='340' side='right'caption='[[1pys]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='1pys' size='340' side='right'caption='[[1pys]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1pys]] is a 2 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=1PYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PYS FirstGlance]. <br>
<table><tr><td colspan='2'>[[1pys]] 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=1PYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PYS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phenylalanine--tRNA_ligase Phenylalanine--tRNA ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.20 6.1.1.20] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1pys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pys OCA], [https://pdbe.org/1pys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pys RCSB], [https://www.ebi.ac.uk/pdbsum/1pys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pys ProSAT]</span></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=1pys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pys OCA], [https://pdbe.org/1pys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pys RCSB], [https://www.ebi.ac.uk/pdbsum/1pys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pys ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYFA_THET8 SYFA_THET8]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1pys ConSurf].
</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=1pys ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus, solved at 2.9 A resolution, displays (alpha beta)2 subunit organization. Unexpectedly, both the catalytic alpha- and the non-catalytic beta-subunits comprise the characteristic fold of the class II active-site domains. The alpha beta heterodimer contains most of the building blocks so far identified in the class II synthetases. The presence of an RNA-binding domain, similar to that of the U1A spliceosomal protein, in the beta-subunit is indicative of structural relationships among different families of RNA-binding proteins. The structure suggests a plausible catalytic mechanism which explains why the primary site of tRNA aminoacylation is different from that of the other class II enzymes.
Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus.,Mosyak L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG Nat Struct Biol. 1995 Jul;2(7):537-47. PMID:7664121<ref>PMID:7664121</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1pys" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Phenylalanine--tRNA ligase]]
[[Category: Thermus thermophilus HB8]]
[[Category: Thermus thermophilus]]
[[Category: Delarue M]]
[[Category: Delarue, M]]
[[Category: Goldgur Y]]
[[Category: Goldgur, Y]]
[[Category: Mosyak L]]
[[Category: Mosyak, L]]
[[Category: Reshetnikova L]]
[[Category: Reshetnikova, L]]
[[Category: Safro M]]
[[Category: Safro, M]]
[[Category: Aminoacyl-trna synthetase]]
[[Category: Class ii aminoacyl-trna synthetase]]
[[Category: Helix-turn-helix motif]]
[[Category: Phenylalanyl-trna synthetase]]
[[Category: Rbd domain]]
[[Category: Sh3 domain]]

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