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Bacterioferritin from Mycobacterium smegmatis contains zinc in its di-nuclear site

¹ EMBL Hamburg Outstation;
² Weizmann Institute of Science

(RECEIVED February 5, 2008; ACCEPTED April 22, 2008)

Bacterioferritins, also known as cytochrome b1, are oligomeric iron-storage proteins consisting of 24 identical amino acid chains, which form spherical particles consisting of 24 subunits and exhibiting 432 point-group symmetry. They contain one haem b molecule at the interface between two subunits and a di-nuclear metal binding centre. The X-ray structure of bacterioferritin from Mycobacterium smegmatis (Ms-Bfr) was determined to a resolution of 2.7 Å; in the monoclinic space group C2. The asymmetric unit of the crystals contains twelve protein molecules: five dimers and two half-dimers located along the crystallographic twofold axis. Unexpectedly, the di-nuclear metal binding center contains zinc ions instead of the typically observed iron ions in other bacterioferritins.

Keywords: Active sites; Metalloproteins; Electron transport; Structure; Crystallography; bacterioferritin; iron storage; mycobacterium smegmatis

³ E-mail: msweiss{at}embl-hamburg.de

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