9DDD
SufS-SufU complex from Mycobacterium Tuberculosis
Summary for 9DDD
Entry DOI | 10.2210/pdb9ddd/pdb |
Related | 9DCL |
Descriptor | Probable cysteine desulfurase, Possible nitrogen fixation related protein, ALANINE, ... (5 entities in total) |
Functional Keywords | fe-s cluster biogenesis cysteine desulfurase zn binding, biosynthetic protein |
Biological source | Mycobacterium tuberculosis More |
Total number of polymer chains | 4 |
Total formula weight | 125523.67 |
Authors | |
Primary citation | Stuteley, S.M.,Chen, J.,Wang, J.,Dawes, S.,Baker, E.N.,Squire, C.J.,Pandelia, M.E.,Bashiri, G. Feedback regulation of iron-sulfur cluster biogenesis. Biorxiv, 2025 Cited by PubMed Abstract: Iron-sulfur (Fe-S) clusters are ubiquitous cofactors in biological systems. Given their central role in bacterial metabolism and pathogenesis, the biogenesis of Fe-S clusters is tightly controlled. We reveal a feedback regulatory mechanism involving the sulfide producing SufS/SufU complex within the sulfur utilization (SUF) system of , the bacterium that causes tuberculosis. In this mechanism, [2Fe-2S] clusters compete with zinc ions for binding to the sulfide transfer protein SufU. Cluster binding induces SufU tetramerization, which prevents its interaction with the cysteine desulfurase SufS, thereby inhibiting SufS activation and limiting sulfide supply for Fe-S cluster biogenesis. These findings uncover an unrecognized regulatory mechanism in , ensuring strict control of Fe-S cluster production. PubMed: 40667192DOI: 10.1101/2025.06.15.659787 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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