1NF4

X-Ray Structure of the Desulfovibrio desulfuricans bacterioferritin: the diiron site in different states (reduced structure)

Summary for 1NF4

• Entry DOI: 10.2210/pdb1nf4/pdb
• Descriptor: bacterioferritin, FE (II) ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: bacterioferritin, active as 24-mer, diiron centre, fe-coproporphyrin iii haem cofactor, iron storage-electron transport complex, iron storage/electron transport
• Biological source: Desulfovibrio desulfuricans
• Total number of polymer chains: 16
• Total formula weight: 331335.37

Authors

Macedo, S.,Romao, C.V.,Mitchell, E.,Matias, P.M.,Liu, M.Y.,Xavier, A.V.,LeGall, J.,Teixeira, M.,Lindley, P.,Carrondo, M.A. (deposition date: 2002-12-13, release date: 2003-04-01, Last modification date: 2024-04-03)

Primary citation

Macedo, S.,Romao, C.V.,Mitchell, E.,Matias, P.M.,Liu, M.Y.,Xavier, A.V.,LeGall, J.,Teixeira, M.,Lindley, P.,Carrondo, M.A.
The nature of the di-iron site in the bacterioferritin from Desulfovibrio desulfuricans
NAT.STRUCT.BIOL., 10:285-290, 2003

PubMed Abstract: The first crystal structure of a native di-iron center in an iron-storage protein (bacterio)ferritin is reported. The protein, isolated from the anaerobic bacterium Desulfovibrio desulfuricans, has the unique property of having Fe-coproporphyrin III as its heme cofactor. The three-dimensional structure of this bacterioferritin was determined in three distinct catalytic/redox states by X-ray crystallography (at 1.95, 2.05 and 2.35 A resolution), corresponding to different intermediates of the di-iron ferroxidase site. Conformational changes associated with these intermediates support the idea of a route for iron entry into the protein shell through a pore that passes through the di-iron center. Molecular surface and electrostatic potential calculations also suggest the presence of another ion channel, distant from the channels at the three- and four-fold axes proposed as points of entry for the iron atoms.

PubMed: 12627224
DOI: 10.1038/nsb909

Experimental method

X-RAY DIFFRACTION (2.05 Å)