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Published online before print April 29, 2008, 10.1110/ps.034819.108
Protein Science (2008), 17:1138-1150. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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Bacterioferritin from Mycobacterium smegmatis contains zinc in its di-nuclear site

Robert Janowski1, Tamar Auerbach-Nevo2, and Manfred S. Weiss1

1 EMBL Hamburg Outstation, D-22603 Hamburg, Germany
2 Department of Structural Biology, Weizmann Institute of Science, 76100 Rehovot, Israel

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

Bacterioferritins, also known as cytochrome b 1, 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 center. 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 12 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: bacterioferritin; Mycobacterium smegmatis; di-metal site; iron storage; haem


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