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- Title
The nature of the di-iron site in the bacterioferritin from Desulfovibrio desulfuricans.
- Authors
Macedo, Sofia; Romao, Celia V.; Mitchell, Edward; Matias, Pedro M.; Liu, Ming Y.; Xavier, Antonio V.; LeGall, Jean; Teixeira, Miguel; Lindley, Peter; Carrondo, Maria A.
- 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.
- Subjects
FERRITIN; DESULFOVIBRIO
- Publication
Nature Structural Biology, 2003, Vol 10, Issue 4, p285
- ISSN
1072-8368
- Publication type
Article
- DOI
10.1038/nsb909