5erg: Difference between revisions
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<StructureSection load='5erg' size='340' side='right'caption='[[5erg]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='5erg' size='340' side='right'caption='[[5erg]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5erg]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5erg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ERG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ERG 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]] 2.202Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5erg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5erg OCA], [https://pdbe.org/5erg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5erg RCSB], [https://www.ebi.ac.uk/pdbsum/5erg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5erg ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/TRM61_YEAST TRM61_YEAST] Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. GCD14 is also required for repression of GCN4 mRNA translation by the upstream open reading frames (uORFs) under conditions of amino acid sufficiency.<ref>PMID:10779558</ref> <ref>PMID:9539420</ref> <ref>PMID:9851972</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fan | [[Category: Saccharomyces cerevisiae S288C]] | ||
[[Category: Jiang | [[Category: Fan X]] | ||
[[Category: Li | [[Category: Jiang X]] | ||
[[Category: Teng | [[Category: Li X]] | ||
[[Category: Wang | [[Category: Teng M]] | ||
[[Category: Wang | [[Category: Wang C]] | ||
[[Category: Zhu | [[Category: Wang M]] | ||
[[Category: Zhu Y]] | |||
Revision as of 11:18, 12 July 2023
Crystal structure of the two-subunit tRNA m1A58 methyltransferase TRM6-TRM61 in complex with SAMCrystal structure of the two-subunit tRNA m1A58 methyltransferase TRM6-TRM61 in complex with SAM
Structural highlights
FunctionTRM61_YEAST Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. GCD14 is also required for repression of GCN4 mRNA translation by the upstream open reading frames (uORFs) under conditions of amino acid sufficiency.[1] [2] [3] Publication Abstract from PubMedThe N(1) methylation of adenine at position 58 (m(1)A58) of tRNA is an important post-transcriptional modification, which is vital for maintaining the stability of the initiator methionine tRNAi(Met). In eukaryotes, this modification is performed by the TRM6-TRM61 holoenzyme. To understand the molecular mechanism that underlies the cooperation of TRM6 and TRM61 in the methyl transfer reaction, we determined the crystal structure of TRM6-TRM61 holoenzyme from Saccharomyces cerevisiae in the presence and absence of its methyl donor S-Adenosyl-L-methionine (SAM). In the structures, two TRM6-TRM61 heterodimers assemble as a heterotetramer. Both TRM6 and TRM61 subunits comprise an N-terminal beta-barrel domain linked to a C-terminal Rossmann-fold domain. TRM61 functions as the catalytic subunit, containing a methyl donor (SAM) binding pocket. TRM6 diverges from TRM61, lacking the conserved motifs used for binding SAM. However, TRM6 cooperates with TRM61 forming an L-shaped tRNA binding regions. Collectively, our results provide a structural basis for better understanding the m(1)A58 modification of tRNA occurred in Saccharomyces cerevisiae. Crystal structure of the two-subunit tRNA m(1)A58 methyltransferase TRM6-TRM61 from Saccharomyces cerevisiae.,Wang M, Zhu Y, Wang C, Fan X, Jiang X, Ebrahimi M, Qiao Z, Niu L, Teng M, Li X Sci Rep. 2016 Sep 1;6:32562. doi: 10.1038/srep32562. PMID:27582183[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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