4rr6
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==N-terminal editing domain of threonyl-tRNA synthetase from Aeropyrum pernix with L-Ser3AA (snapshot 1)== | |
- | + | <StructureSection load='4rr6' size='340' side='right'caption='[[4rr6]], [[Resolution|resolution]] 1.88Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[4rr6]] 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=4RR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RR6 FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88Å</td></tr> | |
- | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A3S:SERINE-3-AMINOADENOSINE'>A3S</scene></td></tr> |
- | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rr6 OCA], [https://pdbe.org/4rr6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rr6 RCSB], [https://www.ebi.ac.uk/pdbsum/4rr6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rr6 ProSAT]</span></td></tr> |
- | [[Category: | + | </table> |
- | [[Category: | + | == Function == |
- | [[Category: | + | [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> |
- | [[Category: | + | == References == |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Aeropyrum pernix K1]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Ahmad S]] | ||
+ | [[Category: Kamarthapu V]] | ||
+ | [[Category: Muthukumar S]] | ||
+ | [[Category: Sankaranarayanan R]] | ||
+ | [[Category: Yerabham ASK]] |
Current revision
N-terminal editing domain of threonyl-tRNA synthetase from Aeropyrum pernix with L-Ser3AA (snapshot 1)
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