dc.contributor.author | Yao, Huili | |
dc.contributor.author | Wang, Yan | |
dc.contributor.author | Lovell, Scott | |
dc.contributor.author | Kumar, Ritesh | |
dc.contributor.author | Ruvinsky, Anatoly M. | |
dc.contributor.author | Battaile, Kevin P. | |
dc.contributor.author | Vakser, Ilya A. | |
dc.contributor.author | Rivera, Mario | |
dc.date.accessioned | 2017-06-06T18:31:40Z | |
dc.date.available | 2017-06-06T18:31:40Z | |
dc.date.issued | 2012-08-15 | |
dc.identifier.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 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/24386 | |
dc.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. | en_US |
dc.description.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. | en_US |
dc.publisher | American Chemical Society | en_US |
dc.title | The structure of the BfrB-Bfd complex reveals protein-protein interactions enabling iron release from bacterioferritin | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Yao, Huili | |
kusw.kuauthor | Wang, Yan | |
kusw.kuauthor | Lovell, Scott | |
kusw.kuauthor | Kumar, Ritesh | |
kusw.kuauthor | Ruvinsky, Anatoly M. | |
kusw.kuauthor | Battaile, Kevin P. | |
kusw.kuauthor | Vasker, Ilya A. | |
kusw.kuauthor | Rivera, Mario | |
kusw.kudepartment | Chemistry | en_US |
dc.identifier.doi | 10.1021/ja305180n | en_US |
kusw.oaversion | Scholarly/refereed, publisher version | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC3428730 | en_US |
dc.rights.accessrights | openAccess | |