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


ABSTRACT: 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 A 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.

SUBMITTER: Janowski R 

PROVIDER: S-EPMC2442004 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature

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

Janowski Robert R   Auerbach-Nevo Tamar T   Weiss Manfred S MS  

Protein science : a publication of the Protein Society 20080429 7


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 A in the monoclinic space group C2. The as  ...[more]

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