4jwf: Difference between revisions
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==Crystal structure of spTrm10(74)-SAH complex== | ==Crystal structure of spTrm10(74)-SAH complex== | ||
<StructureSection load='4jwf' size='340' side='right' caption='[[4jwf]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='4jwf' size='340' side='right'caption='[[4jwf]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jwf]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4jwf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JWF FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=4jwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jwf OCA], [https://pdbe.org/4jwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jwf RCSB], [https://www.ebi.ac.uk/pdbsum/4jwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jwf 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/TRM10_SCHPO TRM10_SCHPO] Catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNAs (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[TRNA methyltransferase|TRNA methyltransferase]] | *[[TRNA methyltransferase 3D structures|TRNA methyltransferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Schizosaccharomyces pombe 972h-]] | ||
[[Category: | [[Category: Shao Z]] | ||
[[Category: | [[Category: Yan W]] | ||
Revision as of 14:28, 30 November 2022
Crystal structure of spTrm10(74)-SAH complexCrystal structure of spTrm10(74)-SAH complex
Structural highlights
FunctionTRM10_SCHPO Catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNAs (By similarity). Publication Abstract from PubMedTransfer RNA (tRNA) methylation is necessary for the proper biological function of tRNA. The N1 methylation of guanine at Position 9 (m1G9) of tRNA, which is widely identified in eukaryotes and archaea, was found to be catalyzed by the Trm10 family of methyltransferases (MTases). Here, we report the first crystal structures of the tRNA MTase spTrm10 from Schizosaccharomyces pombe in the presence and absence of its methyl donor product S-adenosyl-homocysteine (SAH) and its ortholog scTrm10 from Saccharomyces cerevisiae in complex with SAH. Our crystal structures indicated that the MTase domain (the catalytic domain) of the Trm10 family displays a typical SpoU-TrmD (SPOUT) fold. Furthermore, small angle X-ray scattering analysis reveals that Trm10 behaves as a monomer in solution, whereas other members of the SPOUT superfamily all function as homodimers. We also performed tRNA MTase assays and isothermal titration calorimetry experiments to investigate the catalytic mechanism of Trm10 in vitro. In combination with mutational analysis and electrophoretic mobility shift assays, our results provide insights into the substrate tRNA recognition mechanism of Trm10 family MTases. Crystal structure of tRNA m1G9 methyltransferase Trm10: insight into the catalytic mechanism and recognition of tRNA substrate.,Shao Z, Yan W, Peng J, Zuo X, Zou Y, Li F, Gong D, Ma R, Wu J, Shi Y, Zhang Z, Teng M, Li X, Gong Q Nucleic Acids Res. 2013 Sep 29. PMID:24081582[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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