Article
Functional Integrity of Radical SAM Enzyme Dph1•Dph2 Requires Non-canonical Cofactor Motifs with Tandem Cysteines
2024-03-26
Abstract excerpt
The Dph1•Dph2 heterodimer from yeast is a radical SAM (RS) enzyme that generates the 3-amino-3-carboxy-propyl (ACP) precursor for diphthamide, a clinically relevant modification on eukaryotic elongation factor 2 (eEF2). ACP formation requires SAM cleavage and atypical Cys-bound Fe-S clusters in each Dph1 and Dph2 subunit. Intriguingly, the first Cys residue in each motif locates next to another, ill-defined cystei...
Topics
Open a Topic to create a Post that cites this publication.
Identifiers and source
- Literature Corpus work
- 610348b8-1b64-5f7c-9c58-16c4ba753544
- DOI
- 10.20944/preprints202403.1547.v1
