1pys
From Proteopedia
(Difference between revisions)
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<StructureSection load='1pys' size='340' side='right'caption='[[1pys]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='1pys' size='340' side='right'caption='[[1pys]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1pys]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| - | <tr id=' | + | <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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, 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: Thermus thermophilus HB8]] | |
| - | [[Category: Thermus thermophilus]] | + | [[Category: Delarue M]] |
| - | [[Category: Delarue | + | [[Category: Goldgur Y]] |
| - | [[Category: Goldgur | + | [[Category: Mosyak L]] |
| - | [[Category: Mosyak | + | [[Category: Reshetnikova L]] |
| - | [[Category: Reshetnikova | + | [[Category: Safro M]] |
| - | [[Category: Safro | + | |
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Current revision
PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS
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