1yi8
From Proteopedia
(Difference between revisions)
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<StructureSection load='1yi8' size='340' side='right'caption='[[1yi8]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1yi8' size='340' side='right'caption='[[1yi8]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1yi8]] is a 3 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1yi8]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YI8 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]] 2.1Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yi8 OCA], [https://pdbe.org/1yi8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yi8 RCSB], [https://www.ebi.ac.uk/pdbsum/1yi8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yi8 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/SYW2_DEIRA SYW2_DEIRA] Catalyzes the formation of 5'adenyl-Trp and tRNA(Trp) but with 5-fold less activity than TrpRS. Increases the solubility of the nitric oxide synthase oxygenase (nos), as well as its affinity for substrate L-arginine and its nitric-oxide synthase activity. The complex between trpS2 and nos catalyzes the regioselective nitration of tryptophan at the 4-position. |
== 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=1yi8 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=1yi8 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The most divergent of two tryptophanyl tRNA synthetases (TrpRS II) found in Deinococcus radiodurans interacts with a nitric oxide synthase protein that produces 4-nitro-tryptophan (4-NRP). TrpRS II efficiently charges transfer RNA(Trp) with 4-NRP and 5-hydroxy-tryptophan (5-HRP). The crystal structures of TrpRS II bound to tryptophan and 5-HRP reveal residue substitutions that accommodate modified indoles. A class of auxiliary bacterial TrpRSs conserve this capacity to charge tRNA with nonstandard amino acids. | ||
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| - | Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan.,Buddha MR, Crane BR Nat Struct Mol Biol. 2005 Mar;12(3):274-5. Epub 2005 Feb 20. PMID:15723076<ref>PMID:15723076</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1yi8" 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: | + | [[Category: Deinococcus radiodurans R1]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Buddha | + | [[Category: Buddha MR]] |
| - | [[Category: Crane | + | [[Category: Crane BR]] |
| - | + | ||
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Current revision
Crystal structure of tryptophanyl trRNA synthetase II from Deinococcus radiodurans in complex with L-Trp
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