Complete assignment of the 1H nuclear magnetic resonance spectrum of French bean plastocyanin. Sequential resonance assignments, secondary structure and global fold.
Complete assignment of the 1H nuclear magnetic resonance spectrum of French bean plastocyanin. Sequential resonance assignments, secondary structure and global fold.
复制标题
法国豆质体蓝素的 1H 核磁共振谱的完整分配。
DOI：
10.1016/0022-2836(88)90291-4
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发表时间：
1988
影响因子：
5.6
通讯作者：
Wright,PE
中科院分区：
文献类型：
--
作者：
Chazin,WJ;Wright,PE
序列特异性质子核磁共振(n.m.r.)对四季豆铜(I)叶绿体蓝素的99个氨基酸残基进行了归属。这些分配是使用标准的顺序分配程序进行的，并因可获得完整的自旋系统分配而大大便利。主链质子之间的特征短NOE连接性、3JHNα的值以及主链酰胺质子缓慢交换的位置，识别和定义了规则二级结构的元素。可以毫不含糊地识别出八条定义明确的β链、一小段螺旋和八个紧密转弯。在一组非常广泛的链间NOE连接性的基础上，β-链可以被包装成两个不同的β-片。蛋白质中80%以上的残基可以分配到二级结构的某些规则元素上。Nm.r.数据足以定义链折叠拓扑，这是希腊关键的β-Barrel的拓扑，并提供了对全局折叠的定性描述。菜豆叶绿体花青素在溶液中的整体结构与杨树叶绿体花青素的晶体结构非常相似。然而，观察到显著的局部差异，特别是在连接一些β链的环中。
Sequence-specific proton nuclear magnetic resonance (n.m.r.) assignments for all 99 amino acid residues of French bean Cu(I) plastocyanin are described. The assignments were made using standard sequential assignment procedures and were greatly facilitated by the availability of complete spin system assignments. The characteristic short NOE connectivities between backbone protons, the values of3JHNα, and the locations of slowly exchanging backbone amide protons, identify and define the elements of regular secondary structure. Eight well-defined β-strands, a small helical segment and eight tight turns can be identified unambiguously. On the basis of a very extensive set of inter-strand NOE connectivities, the β-strands can be packed into two distinct β-sheets. Over 80% of the residues in the protein can be assigned to some regular element of secondary structure. The n.m.r. data is sufficient to define the chain folding topology, which is that of a Greek key β-barrel, and provides a qualitative description of the global fold. The overall structure of French bean plastocyanin in solution is very similar to that of poplar plastocyanin in crystals. Significant local differences are, however, observed, particularly in the loops connecting some of the β-strands.