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The structure of the BfrB-Bfd complex reveals protein-protein interactions enabling iron release from bacterioferritin. | LitMetric

AI Article Synopsis

  • Ferritin-like molecules play a crucial role in iron storage and homeostasis, allowing for storage at much higher concentrations than normally possible with iron.
  • The study presents the X-ray crystal structure of Pseudomonas aeruginosa bacterioferritin (Pa-BfrB) in complex with its partner, bacterioferritin-associated ferredoxin (Pa-Bfd), offering new insights into how iron is mobilized from storage.
  • The structure highlights conserved residues at the interface between Pa-BfrB and Pa-Bfd, indicating a key recognition mechanism that may be important for iron homeostasis in various pathogenic bacteria.

Article Abstract

Ferritin-like molecules are unique to cellular iron homeostasis because they can store iron at concentrations much higher than those dictated by the solubility of Fe(3+). Very little is known about the protein interactions that deliver iron for storage or promote the mobilization of stored iron from ferritin-like molecules. Here, we report the X-ray crystal structure of Pseudomonas aeruginosa bacterioferritin (Pa-BfrB) in complex with bacterioferritin-associated ferredoxin (Pa-Bfd) at 2.0 Å resolution. As the first example of a ferritin-like molecule in complex with a cognate partner, the structure provides unprecedented insight into the complementary interface that enables the [2Fe-2S] cluster of Pa-Bfd to promote heme-mediated electron transfer through the BfrB protein dielectric (~18 Å), a process that is necessary to reduce the core ferric mineral and facilitate mobilization of Fe(2+). The Pa-BfrB-Bfd complex also revealed the first structure of a Bfd, thus providing a first view to what appears to be a versatile metal binding domain ubiquitous to the large Fer2_BFD family of proteins and enzymes with diverse functions. Residues at the Pa-BfrB-Bfd interface are highly conserved in Bfr and Bfd sequences from a number of pathogenic bacteria, suggesting that the specific recognition between Pa-BfrB and Pa-Bfd is of widespread significance to the understanding of bacterial iron homeostasis.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3428730PMC
http://dx.doi.org/10.1021/ja305180nDOI Listing

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