4E6K

2.0 A resolution structure of Pseudomonas aeruginosa bacterioferritin (BfrB) in complex with bacterioferritin associated ferredoxin (Bfd)

Summary for 4E6K

• Entry DOI: 10.2210/pdb4e6k/pdb
• Descriptor: Bacterioferritin, bacterioferritin-associated ferredoxin, POTASSIUM ION, ... (8 entities in total)
• Functional Keywords: protein complex, iron storage, iron binding, iron mobilization, ferritin, iron homeostasis, bacterial iron metabolism, metal binding protein-electron transport complex, metal binding protein/electron transport
• Biological source: Pseudomonas aeruginosa; More
• Total number of polymer chains: 9
• Total formula weight: 137649.71

Authors

Lovell, S.,Battaile, K.P.,Yao, H.,Wang, Y.,Kumar, R.,Ruvinsky, A.,Vasker, I.,Rivera, M. (deposition date: 2012-03-15, release date: 2012-08-01, Last modification date: 2023-09-13)

Primary citation

Yao, H.,Wang, Y.,Lovell, S.,Kumar, R.,Ruvinsky, A.M.,Battaile, K.P.,Vakser, I.A.,Rivera, M.
The Structure of the BfrB-Bfd Complex Reveals Protein-Protein Interactions Enabling Iron Release from Bacterioferritin.
J.Am.Chem.Soc., 134:13470-13481, 2012

PubMed 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.

PubMed: 22812654
DOI: 10.1021/ja305180n

Experimental method

X-RAY DIFFRACTION (2 Å)