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TitleThe structure of the SufBCD-SufE complex reveals the mechanism of sulfur transfer in bacterial Fe-S cluster assembly.
Journal, issue, pagesbioRxiv, Year 2026
Publish dateMay 19, 2026
AuthorsNidhi Chhikara / Nadia Mireku / Jack A Dunkle / Patrick A Frantom /
PubMed AbstractIron-sulfur clusters are essential cofactors assembled in bacteria by the Suf pathway through a series of transient protein-protein interactions that transfer sulfur from L-cysteine to a scaffold ...Iron-sulfur clusters are essential cofactors assembled in bacteria by the Suf pathway through a series of transient protein-protein interactions that transfer sulfur from L-cysteine to a scaffold complex. While early steps in persulfide transfer are well characterized, the mechanism of sulfur delivery to the SufBCD scaffold has remained unresolved. Here, we report the first structure of the SufBCD-SufE complex, capturing the final step in persulfide transfer in the Suf pathway. The structure reveals coordinated conformational changes in both SufB and SufE that expose the otherwise buried C254 acceptor site and position the SufE C51 loop beneath the SufB-SufD axis. Biochemical analysis of SufB variants demonstrates that substitutions in the globally conserved 220s β-strand enhance SufE binding affinity and persulfide transfer rates, consistent with stabilization of a locally rearranged, transfer-competent conformation. Together, these results support a model in which conformational gating regulates persulfide transfer, providing a mechanism for controlling access to reactive sulfur intermediates.
External linksbioRxiv / PubMed:42239212 / PubMed Central
MethodsEM (single particle)
Resolution4.21 Å
Structure data

75839

11mp

EMDB-75839, PDB-11mp:
E. coli SufE bound to SufBC2D
Method: EM (single particle) / Resolution: 4.21 Å

Source
  • escherichia coli (E. coli)
KeywordsMETAL BINDING PROTEIN / Fe-S / Suf pathway / persulfide / iron-sulfur / sulfur transfer

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