5A7T

Crystal structure of Sulfolobus acidocaldarius Trm10 at 2.4 angstrom resolution.

Summary for 5A7T

• Entry DOI: 10.2210/pdb5a7t/pdb
• Descriptor: TRNA (ADENINE(9)-N1)-METHYLTRANSFERASE, DI(HYDROXYETHYL)ETHER (3 entities in total)
• Functional Keywords: transferase, spout, trm10, trna methyltransferase
• Biological source: SULFOLOBUS ACIDOCALDARIUS
• Cellular location: Cytoplasm : Q4J894
• Total number of polymer chains: 1
• Total formula weight: 30640.68

Authors

Van Laer, B.,Roovers, M.,Wauters, L.,Kasprzak, J.,Dyzma, M.,Deyaert, E.,Feller, A.,Bujnicki, J.,Droogmans, L.,Versees, W. (deposition date: 2015-07-09, release date: 2016-01-13, Last modification date: 2024-10-16)

Primary citation

Van Laer, B.,Roovers, M.,Wauters, L.,Kasprzak, J.M.,Dyzma, M.,Deyaert, E.,Kumar Singh, R.,Feller, A.,Bujnicki, J.M.,Droogmans, L.,Versees, W.
Structural and Functional Insights Into tRNA Binding and Adenosine N1-Methylation by an Archaeal Trm10 Homologue.
Nucleic Acids Res., 44:940-, 2016

PubMed Abstract: 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.

PubMed: 26673726
DOI: 10.1093/NAR/GKV1369

Experimental method

X-RAY DIFFRACTION (2.4 Å)