5a7y: Difference between revisions
New page: '''Unreleased structure''' The entry 5a7y is ON HOLD until Paper Publication Authors: Van Laer, B., Roovers, M., Wauters, L., Kasprzak, J., Dyzma, M., Deyaert, E., Feller, A., Bujnicki,... |
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==Crystal structure of Sulfolobus acidocaldarius Trm10 in complex with S-adenosylhomocysteine== | |||
<StructureSection load='5a7y' size='340' side='right'caption='[[5a7y]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5a7y]] is a 2 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=5A7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A7Y FirstGlance]. <br> | |||
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=5a7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a7y OCA], [https://pdbe.org/5a7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a7y RCSB], [https://www.ebi.ac.uk/pdbsum/5a7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a7y ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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;"> | |||
== 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<ref>PMID:26673726</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5a7y" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[TRNA methyltransferase 3D structures|TRNA methyltransferase 3D structures]] | ||
[[Category: Dyzma | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Sulfolobus acidocaldarius]] | ||
[[Category: Bujnicki J]] | |||
[[Category: Deyaert E]] | |||
[[Category: Droogmans L]] | |||
[[Category: Dyzma M]] | |||
[[Category: Feller A]] | |||
[[Category: Kasprzak J]] | |||
[[Category: Roovers M]] | |||
[[Category: Van Laer B]] | |||
[[Category: Versees W]] | |||
[[Category: Wauters L]] | |||
Latest revision as of 14:05, 10 January 2024
Crystal structure of Sulfolobus acidocaldarius Trm10 in complex with S-adenosylhomocysteineCrystal structure of Sulfolobus acidocaldarius Trm10 in complex with S-adenosylhomocysteine
Structural highlights
FunctionTRM10_SULAC Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 9 (m1A9) in tRNA.[1] Publication Abstract from PubMedPurine 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 AlsoReferences
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