4rrb: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==N-terminal editing domain of threonyl-tRNA synthetase from Aeropyrum pernix with L-Thr3AA (snapshot 2)== | ==N-terminal editing domain of threonyl-tRNA synthetase from Aeropyrum pernix with L-Thr3AA (snapshot 2)== | ||
<StructureSection load='4rrb' size='340' side='right' caption='[[4rrb]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='4rrb' size='340' side='right'caption='[[4rrb]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4rrb]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4rrb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix_K1 Aeropyrum pernix K1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RRB FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A3T:3-DEOXY-3-(L-THREONYLAMINO)ADENOSINE'>A3T</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A3T:3-DEOXY-3-(L-THREONYLAMINO)ADENOSINE'>A3T</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=4rrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rrb OCA], [https://pdbe.org/4rrb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rrb RCSB], [https://www.ebi.ac.uk/pdbsum/4rrb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rrb ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/SYTE_AERPE SYTE_AERPE] Freestanding tRNA editing subunit of threonine--tRNA ligase, the catalytic subunit is probably AC Q9YDW0. Deacylates (edits) mischarged L-seryl-tRNA(Thr) in trans; has no activity on correctly charged L-threonyl-tRNA(Thr) (PubMed:26113036). Probably does not aminoacylate tRNA(Thr) (By similarity). Deacylates correctly charged glycyl-tRNA(Gly), but not glycyl-tRNA(Gly)(2'-dA76) (the terminal 2'-OH of tRNA adenine 76 has been dehydroxylated) nor the 2'-fluoro tRNA derivative, strongly suggesting the editing function is catalyzed by the 2'-OH of A76 of tRNA(Thr) (PubMed:26113036).[UniProtKB:Q980D1]<ref>PMID:26113036</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 23: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aeropyrum pernix K1]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Ahmad | [[Category: Ahmad S]] | ||
[[Category: Kamarthapu | [[Category: Kamarthapu V]] | ||
[[Category: Muthukumar | [[Category: Muthukumar S]] | ||
[[Category: Sankaranarayanan | [[Category: Sankaranarayanan R]] | ||
[[Category: Yerabham | [[Category: Yerabham ASK]] | ||
Revision as of 11:25, 8 March 2023
N-terminal editing domain of threonyl-tRNA synthetase from Aeropyrum pernix with L-Thr3AA (snapshot 2)N-terminal editing domain of threonyl-tRNA synthetase from Aeropyrum pernix with L-Thr3AA (snapshot 2)
Structural highlights
FunctionSYTE_AERPE Freestanding tRNA editing subunit of threonine--tRNA ligase, the catalytic subunit is probably AC Q9YDW0. Deacylates (edits) mischarged L-seryl-tRNA(Thr) in trans; has no activity on correctly charged L-threonyl-tRNA(Thr) (PubMed:26113036). Probably does not aminoacylate tRNA(Thr) (By similarity). Deacylates correctly charged glycyl-tRNA(Gly), but not glycyl-tRNA(Gly)(2'-dA76) (the terminal 2'-OH of tRNA adenine 76 has been dehydroxylated) nor the 2'-fluoro tRNA derivative, strongly suggesting the editing function is catalyzed by the 2'-OH of A76 of tRNA(Thr) (PubMed:26113036).[UniProtKB:Q980D1][1] Publication Abstract from PubMedProofreading modules of aminoacyl-tRNA synthetases are responsible for enforcing a high fidelity during translation of the genetic code. They use strategically positioned side chains for specifically targeting incorrect aminoacyl-tRNAs. Here, we show that a unique proofreading module possessing a D-aminoacyl-tRNA deacylase fold does not use side chains for imparting specificity or for catalysis, the two hallmark activities of enzymes. We show, using three distinct archaea, that a side-chain-stripped recognition site is fully capable of solving a subtle discrimination problem. While biochemical probing establishes that RNA plays the catalytic role, mechanistic insights from multiple high-resolution snapshots reveal that differential remodelling of the catalytic core at the RNA-peptide interface provides the determinants for correct proofreading activity. The functional crosstalk between RNA and protein elucidated here suggests how primordial enzyme functions could have emerged on RNA-peptide scaffolds before recruitment of specific side chains. Specificity and catalysis hardwired at the RNA-protein interface in a translational proofreading enzyme.,Ahmad S, Muthukumar S, Kuncha SK, Routh SB, Yerabham AS, Hussain T, Kamarthapu V, Kruparani SP, Sankaranarayanan R Nat Commun. 2015 Jun 26;6:7552. doi: 10.1038/ncomms8552. PMID:26113036[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||