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首页> 外文期刊>Journal of Molecular Biology >Ectothiorhodospira halophila Ferrocytochrome c_(551): Solution Structure and Comparison with Bacterial Cytochromes c
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Ectothiorhodospira halophila Ferrocytochrome c_(551): Solution Structure and Comparison with Bacterial Cytochromes c

机译：嗜盐单核嗜铁螺旋体铁细胞色素c_（551）：溶液结构和与细菌细胞色素c的比较

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摘要

The solution structure of the Ectothiorhodospira halophila ferrocytochrome c_(551) has been determined. This molecule belongs to a separate class of small bacterial cytochromes c for which no 3D structure has been reported so far. It is characterizedby a very low redox potential (58 mV) and is isolated from the periplasm of halophilic purple phototrophic bacteria. For the 78 residue protein, 1445 NOE derived distance constraints were used in a combined simulated annealing/restrained molecular dynamics calculation. The final ensemble of 37 structures presents a backbone r.m.s.d. of less than 0.5 A compared to the mean structure. The physical viability of these structures was investigated by subjecting eight of them to a constraint free molecular dynamics simulation. No systematic confor-mational change was observed and the average backbone r.m.s.d. compared to the initial structures was less than 1.5 A. The structure of the E. halophila cytochrome c_(551) shows a striking resemblance to Azotobactervinelandii cytochrome c_(551). Significant differences in backbone conformations occur in three small regions which are implicated in solvent protection of the heme propionates and thiomethyl-8. Comparison with Pseudomonas aeruginosa cytochrome c_(551)reveals that only the common cytochrome c core, i.e. three helices, is conserved. The folding of the protein chain around the heme propionates is very different and results in more efficient solvent protection in Ps. aeruginosa. The electrostatic surfaceof E. halcphila cytochrome c_(551) was found to be significantly different from mitochondrial cytochromes c and bacterial cytochromes Ci but similar to that of Ps. aeruginosa cytochrome c_(551).
机译：已经确定了嗜盐嗜铁球菌嗜铁细胞色素c_（551）的溶液结构。该分子属于小细菌细胞色素c的单独类别，到目前为止，尚未报道其3D结构。它的特点是氧化还原电位极低（58 mV），并且从嗜盐紫色光养细菌的周质中分离出来。对于78个残基蛋白，在组合模拟退火/约束分子动力学计算中使用了1445 NOE衍生的距离约束。 37个结构的最终合奏呈现出骨干r.m.s.d.与平均结构相比，小于0.5A。通过对其中的八个结构进行无约束分子动力学模拟，研究了这些结构的物理可行性。没有观察到系统的构象变化，平均骨干r.m.s.d.相比于初始结构，该结构小于1.5A。嗜盐肠杆菌细胞色素c_（551）的结构与固氮蓝细菌细胞色素c_（551）极为相似。骨架构象的显着差异发生在三个小区域，这与血红素丙酸酯和硫代甲基8的溶剂保护有关。与铜绿假单胞菌细胞色素c_（551）的比较表明，仅保留了常见的细胞色素c核心，即三个螺旋。血红素丙酸酯周围的蛋白质链折叠非常不同，可在Ps中提供更有效的溶剂保护。铜绿。发现嗜盐肠球菌细胞色素c_（551）的静电表面与线粒体细胞色素c和细菌细胞色素Ci明显不同，但与Ps相似。铜绿细胞色素c_（551）。

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