TRNA methyltransferase
From Proteopedia
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| - | <StructureSection load=' | + | <StructureSection load='' size='450' side='right' caption='Structure of tRNA methyltransferase for N1 of guanine 37 complex with S-adenosylhomocysteine (PDB entry [[1uak]])' scene='55/553109/Cv/1'> |
== Function == | == Function == | ||
'''tRNA methyltransferase''' (Trm) methylates specific positions on tRNA. tRNA methylation is a post-transcription modification. The methyl donor is S-adenosylmethionine (SAM) and the product is the methylated tRNA and S-adenosylhomocysteine (SAH)<ref>PMID:25626150</ref>. S-adenosylornithine or sinefugin (SFG) is an inhibitor of the reaction. | '''tRNA methyltransferase''' (Trm) methylates specific positions on tRNA. tRNA methylation is a post-transcription modification. The methyl donor is S-adenosylmethionine (SAM) and the product is the methylated tRNA and S-adenosylhomocysteine (SAH)<ref>PMID:25626150</ref>. S-adenosylornithine or sinefugin (SFG) is an inhibitor of the reaction. | ||
Revision as of 04:37, 16 October 2017
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3D structures of tRNA methyltransferase
Updated on 16-October-2017
References
- ↑ Swinehart WE, Jackman JE. Diversity in mechanism and function of tRNA methyltransferases. RNA Biol. 2015;12(4):398-411. doi: 10.1080/15476286.2015.1008358. PMID:25626150 doi:http://dx.doi.org/10.1080/15476286.2015.1008358
- ↑ Ahn HJ, Kim HW, Yoon HJ, Lee BI, Suh SW, Yang JK. Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition. EMBO J. 2003 Jun 2;22(11):2593-603. PMID:12773376 doi:10.1093/emboj/cdg269
