1g59: Difference between revisions
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<StructureSection load='1g59' size='340' side='right'caption='[[1g59]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1g59' size='340' side='right'caption='[[1g59]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1g59]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G59 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1g59]] is a 4 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=1G59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G59 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]] 2.4Å</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=1g59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g59 OCA], [https://pdbe.org/1g59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g59 RCSB], [https://www.ebi.ac.uk/pdbsum/1g59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g59 ProSAT], [https://www.topsan.org/Proteins/RSGI/1g59 TOPSAN]</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=1g59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g59 OCA], [https://pdbe.org/1g59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g59 RCSB], [https://www.ebi.ac.uk/pdbsum/1g59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g59 ProSAT], [https://www.topsan.org/Proteins/RSGI/1g59 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SYE_THET8 SYE_THET8] 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).<ref>PMID:11224561</ref> <ref>PMID:17161369</ref> | |||
== 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: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermus thermophilus]] | ||
[[Category: | [[Category: Nureki O]] | ||
[[Category: Sekine | [[Category: Sekine S]] | ||
[[Category: Shimada | [[Category: Shimada A]] | ||
[[Category: Vassylyev | [[Category: Vassylyev DG]] | ||
[[Category: Yokoyama | [[Category: Yokoyama S]] | ||
Latest revision as of 14:04, 2 August 2023
GLUTAMYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(GLU).GLUTAMYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(GLU).
Structural highlights
FunctionSYE_THET8 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).[1] [2] 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 PubMedGlutamyl-tRNA synthetases (GluRSs) are divided into two distinct types, with regard to the presence or absence of glutaminyl-tRNA synthetase (GlnRS) in the genetic translation systems. In the original 19-synthetase systems lacking GlnRS, the 'non-discriminating' GluRS glutamylates both tRNAGlu and tRNAGln. In contrast, in the evolved 20-synthetase systems with GlnRS, the 'discriminating' GluRS aminoacylates only tRNAGlu. Here we report the 2.4 A resolution crystal structure of a 'discriminating' GluRS.tRNAGlu complex from Thermus thermophilus. The GluRS recognizes the tRNAGlu anticodon bases via two alpha-helical domains, maintaining the base stacking. We show that the discrimination between the Glu and Gln anticodons (34YUC36 and 34YUG36, respectively) is achieved by a single arginine residue (Arg 358). The mutation of Arg 358 to Gln resulted in a GluRS that does not discriminate between the Glu and Gln anticodons. This change mimics the reverse course of GluRS evolution from anticodon 'non-dicsriminating' to 'discriminating'. Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase.,Sekine S, Nureki O, Shimada A, Vassylyev DG, Yokoyama S Nat Struct Biol. 2001 Mar;8(3):203-6. PMID:11224561[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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