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| | ==Crystal structure of Sulfolobus acidocaldarius Trm10 at 2.4 angstrom resolution.== | | ==Crystal structure of Sulfolobus acidocaldarius Trm10 at 2.4 angstrom resolution.== |
| - | <StructureSection load='5a7t' size='340' side='right' caption='[[5a7t]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='5a7t' size='340' side='right'caption='[[5a7t]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5a7t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33909 Atcc 33909]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A7T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5a7t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A7T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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='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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/tRNA_(adenine(9)-N(1))-methyltransferase tRNA (adenine(9)-N(1))-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.218 2.1.1.218] </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=5a7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a7t OCA], [https://pdbe.org/5a7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a7t RCSB], [https://www.ebi.ac.uk/pdbsum/5a7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a7t 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=5a7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a7t OCA], [http://pdbe.org/5a7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a7t RCSB], [http://www.ebi.ac.uk/pdbsum/5a7t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a7t ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TRM10_SULAC TRM10_SULAC]] Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 9 (m1A9) in tRNA.<ref>PMID:20525789</ref> | + | [https://www.uniprot.org/uniprot/TRM10_SULAC TRM10_SULAC] Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 9 (m1A9) in tRNA.<ref>PMID:20525789</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5a7t" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5a7t" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[TRNA methyltransferase 3D structures|TRNA methyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 33909]] | + | [[Category: Large Structures]] |
| - | [[Category: Bujnicki, J]] | + | [[Category: Sulfolobus acidocaldarius]] |
| - | [[Category: Deyaert, E]] | + | [[Category: Bujnicki J]] |
| - | [[Category: Droogmans, L]] | + | [[Category: Deyaert E]] |
| - | [[Category: Dyzma, M]] | + | [[Category: Droogmans L]] |
| - | [[Category: Feller, A]] | + | [[Category: Dyzma M]] |
| - | [[Category: Kasprzak, J]] | + | [[Category: Feller A]] |
| - | [[Category: Laer, B Van]] | + | [[Category: Kasprzak J]] |
| - | [[Category: Roovers, M]] | + | [[Category: Roovers M]] |
| - | [[Category: Versees, W]] | + | [[Category: Van Laer B]] |
| - | [[Category: Wauters, L]] | + | [[Category: Versees W]] |
| - | [[Category: Spout]]
| + | [[Category: Wauters L]] |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Trm10]]
| + | |
| - | [[Category: Trna methyltransferase]]
| + | |
| Structural highlights
Function
TRM10_SULAC Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 9 (m1A9) in tRNA.[1]
Publication Abstract from PubMed
Purine nucleosides on position 9 of eukaryal and archaeal tRNAs are frequently modified in vivo by the post-transcriptional addition of a methyl group on their N1 atom. The methyltransferase Trm10 is responsible for this modification in both these domains of life. While certain Trm10 orthologues specifically methylate either guanosine or adenosine at position 9 of tRNA, others have a dual specificity. Until now structural information about this enzyme family was only available for the catalytic SPOUT domain of Trm10 proteins that show specificity toward guanosine. Here, we present the first crystal structure of a full length Trm10 orthologue specific for adenosine, revealing next to the catalytic SPOUT domain also N- and C-terminal domains. This structure hence provides crucial insights in the tRNA binding mechanism of this unique monomeric family of SPOUT methyltransferases. Moreover, structural comparison of this adenosine-specific Trm10 orthologue with guanosine-specific Trm10 orthologues suggests that the N1 methylation of adenosine relies on additional catalytic residues.
Structural and functional insights into tRNA binding and adenosine N1-methylation by an archaeal Trm10 homologue.,Van Laer B, Roovers M, Wauters L, Kasprzak JM, Dyzma M, Deyaert E, Kumar Singh R, Feller A, Bujnicki JM, Droogmans L, Versees W Nucleic Acids Res. 2015 Dec 15. pii: gkv1369. PMID:26673726[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kempenaers M, Roovers M, Oudjama Y, Tkaczuk KL, Bujnicki JM, Droogmans L. New archaeal methyltransferases forming 1-methyladenosine or 1-methyladenosine and 1-methylguanosine at position 9 of tRNA. Nucleic Acids Res. 2010 Oct;38(19):6533-43. doi: 10.1093/nar/gkq451. Epub 2010, Jun 4. PMID:20525789 doi:http://dx.doi.org/10.1093/nar/gkq451
- ↑ Van Laer B, Roovers M, Wauters L, Kasprzak JM, Dyzma M, Deyaert E, Kumar Singh R, Feller A, Bujnicki JM, Droogmans L, Versees W. Structural and functional insights into tRNA binding and adenosine N1-methylation by an archaeal Trm10 homologue. Nucleic Acids Res. 2015 Dec 15. pii: gkv1369. PMID:26673726 doi:http://dx.doi.org/10.1093/nar/gkv1369
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