1BFR

IRON STORAGE AND ELECTRON TRANSPORT

Summary for 1BFR

• Entry DOI: 10.2210/pdb1bfr/pdb
• Descriptor: BACTERIOFERRITIN, MANGANESE (II) ION, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: electron transport, iron storage
• Biological source: Escherichia coli
• Total number of polymer chains: 24
• Total formula weight: 454467.25

Authors

Dautant, A.,Yariv, J.,Meyer, J.B.,Precigoux, G.,Sweet, R.M.,Frolow, F.,Kalb(Gilboa), A.J. (deposition date: 1994-12-16, release date: 1996-06-20, Last modification date: 2024-02-07)

Primary citation

Dautant, A.,Meyer, J.B.,Yariv, J.,Precigoux, G.,Sweet, R.M.,Kalb, A.J.,Frolow, F.
Structure of a monoclinic crystal from of cyctochrome b1 (Bacterioferritin) from E. coli.
Acta Crystallogr.,Sect.D, 54:16-24, 1998

PubMed Abstract: Crystals of E. coli cytochrome b1, alias bacterioferritin, were grown fr om a low ionic strength solution. The resulting monoclniic P21 structure was solved by molecular replacement and refined using noncrystallographi c symmetries applied to the fundamental unit, consisting of two protein subunits and a single haem. From the Patterson self-rotation results it was shown that the asymmetric unit of the monoclinic crystal consists of 12 such dimers and corresponds to a complete, nearly spherical, molecule of bacterioferritin (M4 = 450 kDa) of 432 point-group symmetry. It is thus the most symmetrical cytochrome. As previously determined for the tetragonal form, the haem is located in a special position on a local twofold axis of the dimer. A bimetal centre is also observed within the four-helix bundle of each monomer; a metal-binding site is located on the fourfold axis.

PubMed: 9867433
DOI: 10.1107/S0907444997006811

Experimental method

X-RAY DIFFRACTION (2.94 Å)