1bfr
From Proteopedia
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IRON STORAGE AND ELECTRON TRANSPORT
Overview
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.
About this Structure
1BFR is a Single protein structure of sequence from Escherichia coli with MN and HEM as ligands. Structure known Active Sites: MA, MB, MC, MD, ME, MF, MG, MH, MI, MJ, MK, ML, MM, MN, MO, MP, MQ, MR, MS, MT, MU, MV, MW and MX. Full crystallographic information is available from OCA.
Reference
Structure of a monoclinic crystal from of cyctochrome b1 (Bacterioferritin) from E. coli., Dautant A, Meyer JB, Yariv J, Precigoux G, Sweet RM, Kalb AJ, Frolow F, Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):16-24. PMID:9867433
Page seeded by OCA on Mon Nov 5 14:12:45 2007
