2vdu
From Proteopedia
STRUCTURE OF TRM8-TRM82, THE YEAST TRNA M7G METHYLATION COMPLEX
Structural highlights
Function[TRM82_YEAST] Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.[1] [2] [3] [4] [TRMB_YEAST] Methyltransferase that catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity.[HAMAP-Rule:MF_03055][5] [6] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedLoss of N7-methylguanosine (m7G) modification is involved in the recently discovered rapid tRNA degradation pathway. In yeast, this modification is catalyzed by the heterodimeric complex composed of a catalytic subunit Trm8 and a noncatalytic subunit Trm82. We have solved the crystal structure of Trm8 alone and in complex with Trm82. Trm8 undergoes subtle conformational changes upon Trm82 binding which explains the requirement of Trm82 for activity. Cocrystallization with the S-adenosyl-methionine methyl donor defines the putative catalytic site and a guanine binding pocket. Small-angle X-ray scattering in solution of the Trm8-Trm82 heterodimer in complex with tRNA(Phe) has enabled us to propose a low-resolution structure of the ternary complex which defines the tRNA binding mode of Trm8-Trm82 and the structural elements contributing to specificity. Structure of the yeast tRNA m7G methylation complex.,Leulliot N, Chaillet M, Durand D, Ulryck N, Blondeau K, van Tilbeurgh H Structure. 2008 Jan;16(1):52-61. PMID:18184583[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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