4U3G

Crystal structure of Escherichia coli bacterioferritin mutant D132F

Summary for 4U3G

• Entry DOI: 10.2210/pdb4u3g/pdb
• Descriptor: Bacterioferritin, SULFATE ION (3 entities in total)
• Functional Keywords: iron channel, 4-helix bundle, diiron site, oxidoreductase
• Biological source: Escherichia coli O6:H1
• Total number of polymer chains: 12
• Total formula weight: 224138.23

Authors

Wong, S.G.,Grigg, J.C.,Le Brun, N.E.,Moore, G.R.,Murphy, M.E.P.,Mauk, A.G. (deposition date: 2014-07-21, release date: 2014-12-24, Last modification date: 2023-09-27)

Primary citation

Wong, S.G.,Grigg, J.C.,Le Brun, N.E.,Moore, G.R.,Murphy, M.E.,Mauk, A.G.
The B-type Channel Is a Major Route for Iron Entry into the Ferroxidase Center and Central Cavity of Bacterioferritin.
J.Biol.Chem., 290:3732-3739, 2015

PubMed Abstract: Bacterioferritin is a bacterial iron storage and detoxification protein that is capable of forming a ferric oxyhydroxide mineral core within its central cavity. To do this, iron must traverse the bacterioferritin protein shell, which is expected to occur through one or more of the channels through the shell identified by structural studies. The size and negative electrostatic potential of the 24 B-type channels suggest that they could provide a route for iron into bacterioferritin. Residues at the B-type channel (Asn-34, Glu-66, Asp-132, and Asp-139) of E. coli bacterioferritin were substituted to determine if they are important for iron core formation. A significant decrease in the rates of initial oxidation of Fe(II) at the ferroxidase center and subsequent iron mineralization was observed for the D132F variant. The crystal structure of this variant shows that substitution of residue 132 with phenylalanine caused a steric blockage of the B-type channel and no other material structural perturbation. We conclude that the B-type channel is a major route for iron entry into both the ferroxidase center and the iron storage cavity of bacterioferritin.

PubMed: 25512375
DOI: 10.1074/jbc.M114.623082

Experimental method

X-RAY DIFFRACTION (2 Å)