ArticleNature communications2026
Structural basis of FatB-mediated iron uptake via tyrosine/histidine direct coordination accompanying long-distance domain reorganization.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Iron is an essential cofactor for fundamental biological processes. However, Fe(III) is poorly soluble under aerobic conditions, limiting its bioavailability. To secure this essential nutrient, bacteria release high-affinity siderophores that capture environmental Fe(III) and are subsequently imported into the cell as ferric siderophore complexes. While biochemical studies have characterized siderophore uptake in Bacillus species, atomic-level mechanisms of recognition and coordination remain unclear. Here, we investigate the siderophore-binding protein FatB from Bacillus cereus and its interactions with its siderophore, petrobactin (PB), as well as with ferric petrobactin (FePB) and its ferric photoproduct (FePB
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