Structure of a monoclinic crystal form of cytochrome b1 (bacterioferritin) from E-coli

被引:55
作者
Dautant, A [1 ]
Meyer, JB
Yariv, J
Precigoux, G
Sweet, RM
Kalb, AJ
Frolow, F
机构
[1] Univ Bordeaux 1, ERS133 CNRS, Unite Biophys Struct, F-33405 Talence, France
[2] Brookhaven Natl Lab, Dept Biol, Upton, NY 11973 USA
[3] Fac Chem, Weizmann Inst Sci, Rehovot, Israel
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 1998年 / 54卷
关键词
D O I
10.1107/S0907444997006811
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Crystals of E. coli cytochrome bl, alias bacterioferritin, were grown from a low ionic strength solution. The resulting monoclinic P2(1) structure was solved by molecular replacement and refined using noncrystallographic 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 (M-r = 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.
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页码:16 / 24
页数:9
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