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

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    Yao_2012.pdf (3.412Mb)
    Issue Date
    2012-08-15
    Author
    Yao, Huili
    Wang, Yan
    Lovell, Scott
    Kumar, Ritesh
    Ruvinsky, Anatoly M.
    Battaile, Kevin P.
    Vakser, Ilya A.
    Rivera, Mario
    Publisher
    American Chemical Society
    Type
    Article
    Article Version
    Scholarly/refereed, publisher version
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    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 Fe3+. 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 Fe2+. 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.
    Description
    This document is the Accepted Manuscript version of a Published Work that appeared in final form in the Journal of the American Chemical Society, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://doi.org/10.1021/ja305180n.
    URI
    http://hdl.handle.net/1808/24386
    DOI
    https://doi.org/10.1021/ja305180n
    Collections
    • Chemistry Scholarly Works [616]
    Citation
    Yao, H., Wang, Y., Lovell, S., Kumar, R., Ruvinsky, A. M., Battaile, K. P., … Rivera, M. (2012). The structure of the BfrB-Bfd complex reveals protein-protein interactions enabling iron release from bacterioferritin. Journal of the American Chemical Society, 134(32), 13470–13481. http://doi.org/10.1021/ja305180n

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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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