The structure of the soluble domain of an archaeal Rieske iron-sulfur protein at 1.1 Å resolution
The structure of the soluble domain of an archaeal Rieske iron-sulfur protein at 1.1 Å resolution
复制标题
DOI：
10.1016/s0022-2836(02)00323-6
复制
发表时间：
2002-06-07
影响因子：
5.6
通讯作者：
Ladenstein, R
中科院分区：
文献类型：
--
作者：
Bönisch, H;Schmidt, CL;Ladenstein, R
古细菌Rieske铁硫蛋白的第一个晶体结构，即来自超高温嗜酸硫化叶菌酸热硫化叶菌的Rieske铁硫蛋白II（soxF）的可溶性结构域，已通过多波长异常色散（MAD）解决，并已细化到1.1埃分辨率。SoxF是S细胞质膜末端氧化酶超复合体SoxM的一个亚基。嗜酸热菌结合了细胞色素bc（1）、复合物和细胞色素c氧化酶的特征。在细胞色素a（587）/Rieske亚复合物氧化Caldariella quinone过程中，soxF的[2Fe-2S]簇可能是主要的电子受体。soxF和真核细胞色素bc（1）和B（6）f复合物的Rieske蛋白中[2Fe-2S]簇的几何形状和簇结合位点的结构几乎相同，表明催化机制严格保守。soxF的主要结构域和簇结合结构域的一部分，虽然在结构上相关，但在拓扑结构、非共价相互作用和表面电荷方面显示出显着不同的结构。soxF的发散结构反映了不同的拓扑结构的soxM复合物相比，真核BC复合物和适应的极端环境条件下的超高温嗜酸生物体的外膜表面的蛋白质。(C)2002爱思唯尔科技有限公司版权所有。
The first crystal structure of an archaeal Rieske iron-sulfur protein, the soluble domain of Rieske iron-sulfur protein II (soxF) from the hyperthermo-acidophile Sulfolobus acidocaldarius, has been solved by multiple wavelength anomalous dispersion (MAD) and has been refined to 1.1 Angstrom resolution. SoxF is a subunit of the terminal oxidase super-complex SoxM in the plasma membrane of S. acidocaldarius that combines features of a cytochrome bc(1), complex and a cytochrome c oxidase. The [2Fe-2S] cluster of soxF is most likely the primary electron acceptor during the oxidation of caldariella quinone by the cytochrome a(587)/Rieske subcomplex. The geometry of the [2Fe-2S] cluster and the structure of the cluster-binding site are almost identical in soxF and the Rieske proteins from eucaryal cytochrome bc(1) and b(6)f complexes, suggesting a strict conservation of the catalytic mechanism. The main domain of soxF and part of the cluster-binding domain, though structurally related, show a significantly divergent structure with respect to topology, non-covalent interactions and surface charges. The divergent structure of soxF reflects a different topology of the soxM complex compared to eucaryal bc complexes and the adaptation of the protein to the extreme ambient conditions on the outer membrane surface of a hyperthermo-acidophilic organism. (C) 2002 Elsevier Science Ltd. All rights reserved.