2VDU

Structure of trm8-trm82, THE YEAST TRNA m7G methylation complex

Summary for 2VDU

• Entry DOI: 10.2210/pdb2vdu/pdb
• Related: 2VDV
• Descriptor: TRNA (GUANINE-N(7)-)-METHYLTRANSFERASE-ASSOCIATED WD REPEAT PROTEIN TRM82, TRNA (GUANINE-N(7)-)-METHYLTRANSFERASE, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: s-adenosyl-l-methionine, trna processing, phosphorylation, methyltransferase, m7g, trna, spout mt, wd repeat, transferase
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Total number of polymer chains: 4
• Total formula weight: 162550.07

Authors

Leulliot, N.,Chaillet, M.,Durand, D.,Ulryck, N.,Blondeau, K.,Van Tilbeurgh, H. (deposition date: 2007-10-11, release date: 2007-12-18, Last modification date: 2024-05-08)

Primary citation

Leulliot, N.,Chaillet, M.,Durand, D.,Ulryck, N.,Blondeau, K.,Van Tilbeurgh, H.
Structure of the Yeast tRNA M7G Methylation Complex.
Structure, 16:52-, 2008

PubMed Abstract: Loss 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.

PubMed: 18184583
DOI: 10.1016/J.STR.2007.10.025

Experimental method

X-RAY DIFFRACTION (2.4 Å)