Proton-NMR studies show that the Thr-102 mutant of yeast iso-1-cytochrome c is a typical member of the eukaryotic cytochrome c family.
Proton-NMR studies show that the Thr-102 mutant of yeast iso-1-cytochrome c is a typical member of the eukaryotic cytochrome c family.
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质子核磁共振研究表明，酵母iso-1-细胞色素c的Thr-102突变体是真核细胞色素c家族的典型成员。
DOI：
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发表时间：
1988
期刊：
影响因子：
--
通讯作者：
R. J. Williams
中科院分区：
文献类型：
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作者：
G. Pielak;J. Boyd;G. Moore;R. J. Williams
Thr-102突变体的酵母异-1-细胞色素c是一个有用的系统，在这类重要的电子转移蛋白的结构-功能关系的研究，但很少有人知道它的结构。此外，在酵母异-1-细胞色素c的个别氨基酸残基的分配已经由质子NMR。在这里，我们报告了近一半的氨基酸在减少的Thr-102突变体的酵母异-1-细胞色素c的分配。我们还报告了氧化的Thr-102突变体的分配。而还原的异-1-细胞色素c（N. B。而不是Thr-102突变体），目前关于其溶液结构的结构信息很少，并且没有关于氧化蛋白的信息。也没有关于Thr-102突变体的任一氧化态的结构的信息。还原型Thr-102突变体的化学位移和NOE数据的比较以及该突变体与马心和金枪鱼细胞色素c之间类似残基的顺磁位移的比较表明，Thr-102酵母异-1-细胞色素c的基本折叠和突变位点周围的区域与后两种蛋白中发现的相同。可以得出结论，使用Thr-102突变体的结构功能研究的结果将适用于真核细胞色素c一般。这些知识使我们能够在下一篇论文中继续描述酵母iso-1-细胞色素c的一些突变体。
The Thr-102 mutant of yeast iso-1-cytochrome c is a useful system for the study of structure-function relationships in this important class of electron transfer proteins, but little is known about its structure. Furthermore, few assignments of individual amino acid residues in yeast iso-1-cytochrome c have been made by proton NMR. Here we report assignments for nearly half of the amino acids in the reduced Thr-102 mutant of yeast iso-1-cytochrome c. We also report assignments for the oxidized Thr-102 mutant. While the crystal structure of the reduced iso-1-cytochrome c (N. B. not the Thr-102 mutant) has been reported, there is currently little structural information concerning its solution structure and none concerning the oxidized protein. There is also no information concerning the structure of either oxidation state of the Thr-102 mutant. Comparison of the chemical shift and NOE data for the reduced Thr-102 mutant and comparison of paramagnetic shifts for analogous residues between this mutant and horse-heart and tuna cytochromes c reveal that both the basic fold of Thr-102 yeast iso-1-cytochrome c and the region around the site of the mutation are the same as those found in the latter two proteins. It is concluded that the results from structure function studies using the Thr-102 mutant will be applicable to eukaryotic cytochrome c in general. This knowledge allows us to proceed to a description of some mutants of yeast iso-1-cytochrome c in the next paper.
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影响因子：
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