Bacterioferritin from Mycobacterium smegmatis contains zinc in its di-nuclear site |
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Authors: | Janowski Robert Auerbach-Nevo Tamar Weiss Manfred S |
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Institution: | EMBL Hamburg Outstation, D-22603 Hamburg, Germany. |
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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. |
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Keywords: | bacterioferritin Mycobacterium smegmatis di-metal site iron storage haem |
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