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| | <StructureSection load='2vdu' size='340' side='right'caption='[[2vdu]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2vdu' size='340' side='right'caption='[[2vdu]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vdu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VDU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vdu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VDU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vdv|2vdv]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/tRNA_(guanine(46)-N(7))-methyltransferase tRNA (guanine(46)-N(7))-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.33 2.1.1.33] </span></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=2vdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdu OCA], [https://pdbe.org/2vdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vdu RCSB], [https://www.ebi.ac.uk/pdbsum/2vdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vdu ProSAT]</span></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=2vdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdu OCA], [https://pdbe.org/2vdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vdu RCSB], [https://www.ebi.ac.uk/pdbsum/2vdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vdu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TRM82_YEAST TRM82_YEAST]] Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.<ref>PMID:15811913</ref> <ref>PMID:16387656</ref> <ref>PMID:17382321</ref> <ref>PMID:18184583</ref> [[https://www.uniprot.org/uniprot/TRMB_YEAST TRMB_YEAST]] Methyltransferase that catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity.[HAMAP-Rule:MF_03055]<ref>PMID:16387656</ref> <ref>PMID:17382321</ref>
| + | [https://www.uniprot.org/uniprot/TRM82_YEAST TRM82_YEAST] Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.<ref>PMID:15811913</ref> <ref>PMID:16387656</ref> <ref>PMID:17382321</ref> <ref>PMID:18184583</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Blondeau, K]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Chaillet, M]] | + | [[Category: Blondeau K]] |
| - | [[Category: Durand, D]] | + | [[Category: Chaillet M]] |
| - | [[Category: Leulliot, N]] | + | [[Category: Durand D]] |
| - | [[Category: Tilbeurgh, H Van]]
| + | [[Category: Leulliot N]] |
| - | [[Category: Ulryck, N]] | + | [[Category: Ulryck N]] |
| - | [[Category: M7g]] | + | [[Category: Van Tilbeurgh H]] |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: S-adenosyl-l-methionine]]
| + | |
| - | [[Category: Spout mt]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Trna]]
| + | |
| - | [[Category: Trna processing]]
| + | |
| - | [[Category: Wd repeat]]
| + | |
| Structural highlights
Function
TRM82_YEAST Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Loss of N7-methylguanosine (m7G) modification is involved in the recently discovered rapid tRNA degradation pathway. In yeast, this modification is catalyzed by the heterodimeric complex composed of a catalytic subunit Trm8 and a noncatalytic subunit Trm82. We have solved the crystal structure of Trm8 alone and in complex with Trm82. Trm8 undergoes subtle conformational changes upon Trm82 binding which explains the requirement of Trm82 for activity. Cocrystallization with the S-adenosyl-methionine methyl donor defines the putative catalytic site and a guanine binding pocket. Small-angle X-ray scattering in solution of the Trm8-Trm82 heterodimer in complex with tRNA(Phe) has enabled us to propose a low-resolution structure of the ternary complex which defines the tRNA binding mode of Trm8-Trm82 and the structural elements contributing to specificity.
Structure of the yeast tRNA m7G methylation complex.,Leulliot N, Chaillet M, Durand D, Ulryck N, Blondeau K, van Tilbeurgh H Structure. 2008 Jan;16(1):52-61. PMID:18184583[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Alexandrov A, Grayhack EJ, Phizicky EM. tRNA m7G methyltransferase Trm8p/Trm82p: evidence linking activity to a growth phenotype and implicating Trm82p in maintaining levels of active Trm8p. RNA. 2005 May;11(5):821-30. Epub 2005 Apr 5. PMID:15811913 doi:http://dx.doi.org/rna.2030705
- ↑ Alexandrov A, Chernyakov I, Gu W, Hiley SL, Hughes TR, Grayhack EJ, Phizicky EM. Rapid tRNA decay can result from lack of nonessential modifications. Mol Cell. 2006 Jan 6;21(1):87-96. PMID:16387656 doi:http://dx.doi.org/S1097-2765(05)01731-4
- ↑ Matsumoto K, Toyooka T, Tomikawa C, Ochi A, Takano Y, Takayanagi N, Endo Y, Hori H. RNA recognition mechanism of eukaryote tRNA (m7G46) methyltransferase (Trm8-Trm82 complex). FEBS Lett. 2007 Apr 17;581(8):1599-604. Epub 2007 Mar 16. PMID:17382321 doi:http://dx.doi.org/S0014-5793(07)00277-3
- ↑ Leulliot N, Chaillet M, Durand D, Ulryck N, Blondeau K, van Tilbeurgh H. Structure of the yeast tRNA m7G methylation complex. Structure. 2008 Jan;16(1):52-61. PMID:18184583 doi:http://dx.doi.org/S0969-2126(07)00471-6
- ↑ Leulliot N, Chaillet M, Durand D, Ulryck N, Blondeau K, van Tilbeurgh H. Structure of the yeast tRNA m7G methylation complex. Structure. 2008 Jan;16(1):52-61. PMID:18184583 doi:http://dx.doi.org/S0969-2126(07)00471-6
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