The structure of chloroplast cytochrome c6 at 1.9 A resolution: evidence for functional oligomerization.
The structure of chloroplast cytochrome c6 at 1.9 A resolution: evidence for functional oligomerization.
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1.9 A 分辨率下叶绿体细胞色素 c6 的结构:功能性寡聚化的证据。
DOI:
10.1006/jmbi.1995.0404
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发表时间:
1995
期刊:
影响因子:
--
通讯作者:
Yeates,TO
中科院分区:
文献类型:
--
作者:
Kerfeld,CA;Anwar,HP;Interrante,R;Merchant,S;Yeates,TO
The molecular structure of cytochromec6from the green algaChlamydomonas reinhardtiihas been determined from two crystal forms and refined to 1.9 Å resolution. The two crystal forms are likely the result of different levels of post-translational modification of the protein. This is the first report of a high-resolution structure of a chloroplast-derived class Ic-type cytochrome. The overall fold is similar to that of other class Ic-type cytochromes, consisting of a series of α-helices and turns that envelop the heme prosthetic group. There is also a short two-stranded anti-parallel β-sheet in the vicinity of the methionine axial ligand to the heme; this region of the molecule is formed by the most highly conserved residues inc6-type cytochromes. Although class Ic-type cytochromes are assumed to function as monomers, both crystal forms of cytochromec6exhibit oligomerization about the heme crevice that is, in part, mediated by the short anto-parallel β-sheet. The functional significance of this oligomerization is supported by the appearance of similar interfaces in other electron transfer couples. HPLC and light-scattering data, and is furthermore consistent with kinetic data on electron transfer reactions ofc6-type cytochromes.f2