2VXI
The binding of heme and zinc in Escherichia coli Bacterioferritin
Summary for 2VXI
Entry DOI | 10.2210/pdb2vxi/pdb |
Related | 1BCF 1BFR 2HTN |
Descriptor | BACTERIOFERRITIN, PROTOPORPHYRIN IX CONTAINING FE, ZINC ION, ... (5 entities in total) |
Functional Keywords | metal transport, bacterioferritin, iron storage and electron transport, zinc, heme, iron, iron storage, metal-binding |
Biological source | ESCHERICHIA COLI |
Total number of polymer chains | 12 |
Total formula weight | 233969.68 |
Authors | Willies, S.C.,Isupov, M.N.,Garman, E.F.,Littlechild, J.A. (deposition date: 2008-07-04, release date: 2008-11-04, Last modification date: 2024-05-08) |
Primary citation | Willies, S.C.,Isupov, M.N.,Garman, E.F.,Littlechild, J.A. The Binding of Haem and Zinc in the 1.9 A X-Ray Structure of Escherichia Coli Bacterioferritin. J.Biol.Inorg.Chem., 14:201-, 2009 Cited by PubMed Abstract: The crystal structure of Escherichia coli bacterioferritin has been solved to 1.9 A, and shows the symmetrical binding of a haem molecule on the local twofold axis between subunits and a pair of metal atoms bound to each subunit at the ferroxidase centre. These metals have been identified as zinc by the analysis of the structure and X-ray data and confirmed by microfocused proton-induced X-ray emission experiments. For the first time the haem has been shown to be linked to both the internal and the external environments via a cluster of waters positioned above the haem molecule. PubMed: 18946693DOI: 10.1007/S00775-008-0438-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.91 Å) |
Structure validation
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