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| | <StructureSection load='3afh' size='340' side='right'caption='[[3afh]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='3afh' size='340' side='right'caption='[[3afh]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3afh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AFH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3AFH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3afh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AFH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSU:O5-(L-GLUTAMYL-SULFAMOYL)-ADENOSINE'>GSU</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]] 2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate--tRNA_ligase Glutamate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.17 6.1.1.17] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSU:O5-(L-GLUTAMYL-SULFAMOYL)-ADENOSINE'>GSU</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3afh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3afh OCA], [http://pdbe.org/3afh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3afh RCSB], [http://www.ebi.ac.uk/pdbsum/3afh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3afh 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=3afh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3afh OCA], [https://pdbe.org/3afh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3afh RCSB], [https://www.ebi.ac.uk/pdbsum/3afh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3afh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SYE2_THEMA SYE2_THEMA]] Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).[HAMAP-Rule:MF_00022] | + | [https://www.uniprot.org/uniprot/SYE2_THEMA SYE2_THEMA] Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).[HAMAP-Rule:MF_00022] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43589]] | |
| - | [[Category: Glutamate--tRNA ligase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ito, T]] | + | [[Category: Thermotoga maritima]] |
| - | [[Category: Yokoyama, S]] | + | [[Category: Ito T]] |
| - | [[Category: Aminoacyl-trna synthetase]] | + | [[Category: Yokoyama S]] |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Non-discriminating glutamyl-trna synthetase]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Protein biosynthesis]]
| + | |
| - | [[Category: Protein-substrate complex]]
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| Structural highlights
Function
SYE2_THEMA Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).[HAMAP-Rule:MF_00022]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Aminoacyl-tRNA synthetases produce aminoacyl-tRNAs from the substrate tRNA and its cognate amino acid with the aid of ATP. Two types of glutamyl-tRNA synthetase (GluRS) have been discovered: discriminating GluRS (D-GluRS) and nondiscriminating GluRS (ND-GluRS). D-GluRS glutamylates tRNA(Glu) only, while ND-GluRS glutamylates both tRNA(Glu) and tRNA(Gln). ND-GluRS produces the intermediate Glu-tRNA(Gln), which is converted to Gln-tRNA(Gln) by Glu-tRNA(Gln) amidotransferase. Two GluRS homologues from Thermotoga maritima, TM1875 and TM1351, have been biochemically characterized and it has been clarified that only TM1875 functions as an ND-GluRS. Furthermore, the crystal structure of the T. maritima ND-GluRS, TM1875, was determined in complex with a Glu-AMP analogue at 2.0 A resolution. The T. maritima ND-GluRS contains a characteristic structure in the connective-peptide domain, which is inserted into the catalytic Rossmann-fold domain. The glutamylation ability of tRNA(Gln) by ND-GluRS was measured in the presence of the bacterial Glu-tRNA(Gln) amidotransferase GatCAB. Interestingly, the glutamylation efficiency was not affected even in the presence of excess GatCAB. Therefore, GluRS avoids competition with GatCAB and glutamylates tRNA(Gln).
Structure of nondiscriminating glutamyl-tRNA synthetase from Thermotoga maritima.,Ito T, Kiyasu N, Matsunaga R, Takahashi S, Yokoyama S Acta Crystallogr D Biol Crystallogr. 2010 Jul;66(Pt 7):813-20. Epub 2010, Jun 19. PMID:20606262[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ito T, Kiyasu N, Matsunaga R, Takahashi S, Yokoyama S. Structure of nondiscriminating glutamyl-tRNA synthetase from Thermotoga maritima. Acta Crystallogr D Biol Crystallogr. 2010 Jul;66(Pt 7):813-20. Epub 2010, Jun 19. PMID:20606262 doi:10.1107/S0907444910019086
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