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| - | ==Insights into molecular plasticity in protein complexes from Trm9-Trm112 tRNA modifying enzyme crystal structure== | + | ==Structure of Y. lipolytica Trm9-Trm112 complex, a methyltransferase modifying U34 in the anticodon loop of some tRNAs== |
| | <StructureSection load='5cm2' size='340' side='right'caption='[[5cm2]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5cm2' size='340' side='right'caption='[[5cm2]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cm2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_lipolytica Candida lipolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CM2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CM2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5cm2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Yarrowia_lipolytica_CLIB122 Yarrowia lipolytica CLIB122]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CM2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qtt|4qtt]], [[4qtu|4qtu]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YALI0_D12837g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284591 Candida lipolytica]), YALI0_E24761g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284591 Candida lipolytica])</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=5cm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cm2 OCA], [https://pdbe.org/5cm2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cm2 RCSB], [https://www.ebi.ac.uk/pdbsum/5cm2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cm2 ProSAT]</span></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=5cm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cm2 OCA], [http://pdbe.org/5cm2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cm2 RCSB], [http://www.ebi.ac.uk/pdbsum/5cm2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cm2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6C999_YARLI Q6C999_YARLI] |
| | <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: Candida lipolytica]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aleksandrov, A]] | + | [[Category: Yarrowia lipolytica CLIB122]] |
| - | [[Category: Caroline, V]] | + | [[Category: Aleksandrov A]] |
| - | [[Category: Graille, M]] | + | [[Category: Caroline V]] |
| - | [[Category: Lazar, N]] | + | [[Category: Graille M]] |
| - | [[Category: Letoquart, J]] | + | [[Category: Lazar N]] |
| - | [[Category: Liger, D]] | + | [[Category: Letoquart J]] |
| - | [[Category: Tilbeurgh, H Van]] | + | [[Category: Liger D]] |
| - | [[Category: Tran, N van]] | + | [[Category: Van Tilbeurgh H]] |
| - | [[Category: Class i methyltransferase]]
| + | [[Category: Van Tran N]] |
| - | [[Category: Methylation]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Trna methyltransferase]]
| + | |
| Structural highlights
Function
Q6C999_YARLI
Publication Abstract from PubMed
Most of the factors involved in translation (tRNA, rRNA and proteins) are subject to post-transcriptional and post-translational modifications, which participate in the fine-tuning and tight control of ribosome and protein synthesis processes. In eukaryotes, Trm112 acts as an obligate activating platform for at least four methyltransferases (MTase) involved in the modification of 18S rRNA (Bud23), tRNA (Trm9 and Trm11) and translation termination factor eRF1 (Mtq2). Trm112 is then at a nexus between ribosome synthesis and function. Here, we present a structure-function analysis of the Trm9-Trm112 complex, which is involved in the 5-methoxycarbonylmethyluridine (mcm5U) modification of the tRNA anticodon wobble position and hence promotes translational fidelity. We also compare the known crystal structures of various Trm112-MTase complexes, highlighting the structural plasticity allowing Trm112 to interact through a very similar mode with its MTase partners, although those share less than 20% sequence identity.
Insights into molecular plasticity in protein complexes from Trm9-Trm112 tRNA modifying enzyme crystal structure.,Letoquart J, Tran NV, Caroline V, Aleksandrov A, Lazar N, van Tilbeurgh H, Liger D, Graille M Nucleic Acids Res. 2015 Oct 4. pii: gkv1009. PMID:26438534[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Letoquart J, Tran NV, Caroline V, Aleksandrov A, Lazar N, van Tilbeurgh H, Liger D, Graille M. Insights into molecular plasticity in protein complexes from Trm9-Trm112 tRNA modifying enzyme crystal structure. Nucleic Acids Res. 2015 Oct 4. pii: gkv1009. PMID:26438534 doi:http://dx.doi.org/10.1093/nar/gkv1009
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