The structure and heavy-metal-ion-binding sites of horse spleen apoferritin.
The structure and heavy-metal-ion-binding sites of horse spleen apoferritin.
复制标题
马脾去铁铁蛋白的结构和重金属离子结合位点。
DOI:
10.1042/bst0080654
复制
发表时间:
1980
影响因子:
3.9
通讯作者:
P. Harrison
中科院分区:
文献类型:
--
作者:
G. Clegg;R. Stansfield;P. Bourne;P. Harrison
An electron-density map at 0.28 nm (2.8 A) resolution has been calculated for horse spleen apoferritin crystallized in the face-centred cubic space group F432, with a= 18.4 nm (184A)(Banyard et al., 1978). The molecule is a nearly spherical shell [outside and inside diameters respectively 13.0 nm (130A) and 8.0 nm (80A) l formed from 24 equivalent subunits arranged in 432 symmetry. The large cavity is capable of storing up to 4500 Fe (II1) atoms as a microcrystalline inorganic component of approximate composition (FeOOH),(FeO-OPO, H,). The subunits, which lie nearly parallel to threefold and perpendicular to twofold axes, have a cylindrical shape and contain four helices running parallel (or anti-parallel) to the cylinder axis and accounting for about two-thirds of the primary structure. In addition there is a long loop, running over the outside surface of the subunit, that appears to form a short piece of anti-parallel/?-pleated sheet with the loop from its twofoldsymmetry-related neighbour. Connectivities between these regions of secondary structure are not yet clear. The polypeptide backbone of a subunit has been built in a Richards's comparator (Richards, 1968), and a-carbon and carbonyl oxygen co-ordinates have been measured. Positions of the remaining backbone atoms and/?-carbon atoms have been calculated and regularized to standard geometry (Dodson et al., 1976). It is hoped that inclusion of phase information derived from these positions will provide improved electron-density