SOLUTION STRUCTURE OF APOCYTOCHROME B(562)
SOLUTION STRUCTURE OF APOCYTOCHROME B(562)
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DOI：
10.1038/nsb0194-30
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发表时间：
1994-01-01
期刊：
影响因子：
--
通讯作者：
WAND, AJ
中科院分区：
文献类型：
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作者：
FENG, YQ;SLIGAR, SG;WAND, AJ
脱辅基蛋白是许多血红素蛋白折叠途径的重要中间体，但这种中间体的详细结构仍然难以捉摸。在这里，我们提出的脱辅基细胞色素B（562）的结构获得的NMR光谱。脱辅基蛋白具有与全蛋白相似的拓扑结构。然而，两者之间的螺旋-螺旋堆积的显著差异是明显的。在脱辅基蛋白中的血红素结合口袋的大部分被保留，但暴露于溶剂中，产生大的洞穴。由于脱辅基细胞色素B（562）表现出许多熔融球状态的物理特性，这些结果有助于阐明蛋白质熔融球的几种性质的起源。
The apoprotein is an important intermediate on the folding pathways of many haem proteins, yet a detailed structure of such an intermediate has remained elusive. Here we present the structure of apocytochrome b(562) obtained by NMR spectroscopy. The apoprotein has a topology similar to the holoprotein. Nevertheless, significant differences in helix-helix packing between the two are evident. Much of the haem binding pocket in the apoprotein is preserved but exposed to solvent creating a large cavern. As apocytochrome b(562) displays many of the physical characteristics ascribed to the molten globule state, these results help ellucidate the origin of several properties of the protein molten globule.