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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...

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Literature Corpus work
610348b8-1b64-5f7c-9c58-16c4ba753544
DOI
10.20944/preprints202403.1547.v1
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Functional Integrity of Radical SAM Enzyme Dph1•Dph2 Requires Non-canonical Cofactor Motifs with Tandem CysteinesDOI 10.20944/preprints202403.1547.v1
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