1BCF
THE STRUCTURE OF A UNIQUE, TWO-FOLD SYMMETRIC, HAEM-BINDING SITE
Summary for 1BCF
| Entry DOI | 10.2210/pdb1bcf/pdb |
| Descriptor | BACTERIOFERRITIN, MANGANESE (II) ION, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | iron storage and electron transport |
| Biological source | Escherichia coli |
| Total number of polymer chains | 12 |
| Total formula weight | 227233.63 |
| Authors | Frolow, F.,Kalb(Gilboa), A.J.,Yariv, J. (deposition date: 1993-12-06, release date: 1994-12-20, Last modification date: 2024-02-07) |
| Primary citation | Frolow, F.,Kalb, A.J.,Yariv, J. Structure of a unique twofold symmetric haem-binding site. Nat.Struct.Biol., 1:453-460, 1994 Cited by PubMed Abstract: Bacterioferritin of Escherichia coli, also known as cytochrome b1, is a hollow, nearly spherical shell made up of 24 identical protein subunits and 12 haems. We have solved this structure in a tetragonal crystal form at 2.9 A resolution. We find that each haem is bound in a pocket formed by the interface between a pair of symmetry-related subunits. The quasi-twofold axis of the haem is closely aligned with the local twofold axis relating these subunits. The axial ligands of the haem are sulphurs of two equivalent methionyl residues (Met 52) from the symmetry-related subunits. A cluster of four water molecules is trapped in the gap between the upper edge of the haem and two extended protein loops which close off the haem from the outer aqueous environment. This is the first structure of a bis-methionine ligated haem-binding site and the first case of a twofold symmetric haem-binding site. PubMed: 7664064DOI: 10.1038/nsb0794-453 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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