Bisubstrate analogues as structural tools to investigate m⁶A methyltransferase active sites.

ABSTRACT: RNA methyltransferases (MTases) catalyse the transfer of a methyl group to their RNA substrates using most-often S-adenosyl-L-methionine (SAM) as cofactor. Only few RNA-bound MTases structures are currently available due to the difficulties in crystallising RNA:protein complexes. The lack of complex structures results in poorly understood RNA recognition patterns and methylation reaction mechanisms. On the contrary, many cofactor-bound MTase structures are available, resulting in well-understood protein:cofactor recognition, that can guide the design of bisubstrate analogues that mimic the state at which both the substrate and the cofactor is bound. Such bisubstrate analogues were recently synthesized for proteins monomethylating the N6-atom of adenine (m⁶A). These proteins incl

SUBMITTER: Oerum S 

PROVIDER: S-EPMC6546350 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature