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First Step in Catalysis of the Radical S-Adenosylmethionine Methylthiotransferase MiaB Yields an Intermediate with a [3Fe-4S]⁰-Like Auxiliary Cluster.

ABSTRACT: The enzyme MiaB catalyzes the attachment of a methylthio (-SCH₃) group at the C2 position of N⁶-(isopentenyl)adenosine (i⁶A) in the final step of the biosynthesis of the hypermodified tRNA nucleotide 2-methythio-N⁶-(isopentenyl)adenosine (ms²i⁶A). MiaB belongs to the expanding subgroup of enzymes of the radical S-adenosylmethionine (SAM) superfamily that harbor one or more auxiliary [4Fe-4S] clusters in addition to the [4Fe-4S] cluster that all family members require for the reductive cleavage of SAM to afford the common 5'-deoxyadenosyl 5'-radical (5'-dA^•) intermediate. While the role of the radical SAM cluster in generating the 5'-dA^• is well understood, the detailed role of the a

SUBMITTER: Zhang B

PROVIDER: S-EPMC7008301 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature

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Dataset Information

First Step in Catalysis of the Radical S-Adenosylmethionine Methylthiotransferase MiaB Yields an Intermediate with a [3Fe-4S]⁰-Like Auxiliary Cluster.

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OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

First Step in Catalysis of the Radical S-Adenosylmethionine Methylthiotransferase MiaB Yields an Intermediate with a [3Fe-4S]0-Like Auxiliary Cluster.

Publications

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

First Step in Catalysis of the Radical S-Adenosylmethionine Methylthiotransferase MiaB Yields an Intermediate with a [3Fe-4S]⁰-Like Auxiliary Cluster.