7F1E

Structure of METTL6 bound with SAM

Summary for 7F1E

• Entry DOI: 10.2210/pdb7f1e/pdb
• Descriptor: tRNA N(3)-methylcytidine methyltransferase METTL6, S-ADENOSYLMETHIONINE (3 entities in total)
• Functional Keywords: rna methyltransferase, rna, transferase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 67779.37

Authors

Li, S.,Liao, S.,Xu, C. (deposition date: 2021-06-09, release date: 2022-01-12, Last modification date: 2023-11-29)

Primary citation

Li, S.,Zhou, H.,Liao, S.,Wang, X.,Zhu, Z.,Zhang, J.,Xu, C.
Structural basis for METTL6-mediated m3C RNA methylation.
Biochem.Biophys.Res.Commun., 589:159-164, 2021

PubMed Abstract: RNA modifications play important roles in mediating the biological functions of RNAs. 3-methylcytidine (m3C), albeit less abundant, is found to exist extensively in tRNAs, rRNAs and mRNAs. Human METTL6 is a mC methyltransferase for tRNAs, including tRNA. We solved the structure of human METTL6 in the presence of S-adenosyl-L-methionine and found by enzyme assay that recombinant human METTL6 is active towards tRNA. Structural analysis indicated the detailed interactions between S-adenosyl-L-methionine and METTL6, and suggested potential tRNA binding region on the surface of METTL6. The structural research, complemented by biochemistry enzyme assay, will definitely shed light on the design of potent inhibitors for METTL6 in near future.

PubMed: 34922197
DOI: 10.1016/j.bbrc.2021.12.013

Experimental method

X-RAY DIFFRACTION (2.589 Å)