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| | ==Crystal structure of DUF358 protein reveals a putative SPOUT-class rRNA methyltransferase== | | ==Crystal structure of DUF358 protein reveals a putative SPOUT-class rRNA methyltransferase== |
| - | <StructureSection load='3ai9' size='340' side='right' caption='[[3ai9]], [[Resolution|resolution]] 1.55Å' scene=''> | + | <StructureSection load='3ai9' size='340' side='right'caption='[[3ai9]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ai9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AI9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AI9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ai9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AI9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3aia|3aia]]</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=3ai9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ai9 OCA], [https://pdbe.org/3ai9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ai9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ai9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ai9 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MJ1640 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ai9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ai9 OCA], [http://pdbe.org/3ai9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ai9 RCSB], [http://www.ebi.ac.uk/pdbsum/3ai9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ai9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TRMY_METJA TRMY_METJA]] Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs.[HAMAP-Rule:MF_00587]<ref>PMID:22274953</ref> <ref>PMID:22274954</ref> | + | [https://www.uniprot.org/uniprot/TRMY_METJA TRMY_METJA] Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs.[HAMAP-Rule:MF_00587]<ref>PMID:22274953</ref> <ref>PMID:22274954</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: Atcc 43067]] | + | [[Category: Large Structures]] |
| - | [[Category: Chen, H Y]] | + | [[Category: Methanocaldococcus jannaschii]] |
| - | [[Category: Yuan, Y A]] | + | [[Category: Chen HY]] |
| - | [[Category: Mjduf358]] | + | [[Category: Yuan YA]] |
| - | [[Category: Rrna methyltransferase]]
| + | |
| - | [[Category: Spout-class fold]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
TRMY_METJA Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs.[HAMAP-Rule:MF_00587][1] [2]
Publication Abstract from PubMed
The proteins in DUF358 family are all bacterial proteins, which are approximately 200 amino acids long with unknown function. Bioinformatics analysis suggests that these proteins contain several conserved arginines and aspartates that might adopt SPOUT-class fold. Here we report crystal structure of Methanocaldococcus jannaschii DUF358/Mj1640 in complex with S-adenosyl-L-methionine (SAM) at 1.4 A resolution. The structure reveals a single domain structure consisting of eight-stranded beta-sheets sandwiched by six alpha-helices at both sides. Similar to other SPOUT-class members, Mj1640 contains a typical deep trefoil knot at its C-terminus to accommodate the SAM cofactor. However, Mj1640 has limited structural extension at its N-terminus, which is unique to this family member. Mj1640 forms a dimer, which is mediated by two parallel pairs of alpha-helices oriented almost perpendicular to each other. Although Mj1640 shares close structural similarity with Nep1, the significant differences in N-terminal extension domain and the overall surface charge distribution strongly suggest that Mj1640 might target a different RNA sequence. Detailed structural analysis of the SAM-binding pocket reveals that Asp157 or Glu183 from its own monomer or Ser43 from the associate monomer probably plays the catalytic role for RNA methylation.
Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase.,Chen HY, Yuan YA J Mol Cell Biol. 2010 Dec;2(6):366-74. PMID:21098051[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chatterjee K, Blaby IK, Thiaville PC, Majumder M, Grosjean H, Yuan YA, Gupta R, de Crecy-Lagard V. The archaeal COG1901/DUF358 SPOUT-methyltransferase members, together with pseudouridine synthase Pus10, catalyze the formation of 1-methylpseudouridine at position 54 of tRNA. RNA. 2012 Mar;18(3):421-33. doi: 10.1261/rna.030841.111. Epub 2012 Jan 24. PMID:22274953 doi:http://dx.doi.org/10.1261/rna.030841.111
- ↑ Wurm JP, Griese M, Bahr U, Held M, Heckel A, Karas M, Soppa J, Wohnert J. Identification of the enzyme responsible for N1-methylation of pseudouridine 54 in archaeal tRNAs. RNA. 2012 Mar;18(3):412-20. doi: 10.1261/rna.028498.111. Epub 2012 Jan 24. PMID:22274954 doi:http://dx.doi.org/10.1261/rna.028498.111
- ↑ Chen HY, Yuan YA. Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase. J Mol Cell Biol. 2010 Dec;2(6):366-74. PMID:21098051 doi:10.1093/jmcb/mjq034
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