Non-functional conserved residues in globins and their possible role as a folding nucleus.
Non-functional conserved residues in globins and their possible role as a folding nucleus.
复制标题
球蛋白中的非功能性保守残基及其作为折叠核的可能作用。
DOI：
--
复制
发表时间：
1999
影响因子：
5.6
通讯作者：
K. Ting
中科院分区：
文献类型：
--
作者：
O. Ptitsyn;K. Ting
对不同珠蛋白亚家族的 728 个序列进行基于结构的序列比对表明，每个亚家族中都有两簇一致保守的残基。第一个是众所周知的“功能”簇，其中包括六个血红素结合保守残基（Phe CD1、His F8；脂肪族 E11、FG5；疏水性 F4、G5）和七个其他保守残基（Pro C2；脂肪族 H19；疏水性 B10、B13、B14、CD4、E4），这些残基不与血红素结合，但属于其紧邻。这里揭示的第二个簇（脂肪族 A8、G16、G12；芳香族 A12；疏水性 H8，可能还有 H12）远离血红素。它完全是非极性的，并且包括螺旋 A、G 和 H 各一圈（i、i+4 个位置）。众所周知，在脱辅基肌红蛋白折叠的最早阶段形成的 A、G 和 H 螺旋在平衡熔球状态下保持相对稳定，并且在这种状态下很可能彼此紧密堆积。我们已经证明c型细胞色素中存在两个相似的保守簇，即血红素结合簇和远离血红素的簇。 c 细胞色素中的第二簇包括 N 端和 C 端 α 螺旋各一圈。细胞色素c中的这些N端和C端螺旋在蛋白质折叠的最早阶段形成，在熔球状态下保持相对稳定，并且在此状态下彼此紧密堆积，类似于观察到的球蛋白的行为。至少这两个大的蛋白质家族（c型细胞色素和珠蛋白）在非功能性保守残基的存在和相互位置方面具有密切的相似性。我们假设非功能性保守残基是这两个蛋白质家族快速正确折叠成稳定 3D 结构所必需的。
Structure-based sequence alignment of 728 sequences of different globin subfamilies shows that in each subfamily there are two clusters of consensually conserved residues. The first is the well-known "functional" cluster which includes six heme-binding conserved residues (Phe CD1, His F8; aliphatic E11, FG5; hydrophobic F4, G5) and seven other conserved residues (Pro C2; aliphatic H19; hydrophobic B10, B13, B14, CD4, E4) that do not bind the heme but belong to its immediate neighborhood. The second cluster revealed here (aliphatic A8, G16, G12; aromatic A12; hydrophobic H8 and possibly H12) is distant from the heme. It is entirely non-polar and includes one turn (i, i+4 positions) from each of helices A, G, and H. It is known that A, G, and H helices formed at the earliest stage of apomyoglobin folding remain relatively stable in the equilibrium molten globule state, and are likely to be tightly packed with each other in this state. We have shown the existence of two similar conserved clusters in c -type cytochromes, heme-binding and distal from the heme. The second cluster in c -cytochromes includes one turn from each of the N and C-terminal alpha-helices. These N and C-terminal helices in cytochrome c are formed at the earliest stage of protein folding, remain relatively stable in the molten globule state, and are tightly packed with each other in this state, similar to the observed behavior of the globins. At least these two large protein families (c -type cytochromes and globins) have a close similarity in the existence and mutual positions of non-functional conserved residues. We assume that non-functional conserved residues are requisite for the fast and correct folding of both of these protein families into their stable 3D structures.
登录
查看更多内容
天然的三级相互作用稳定了细胞色素 c 的 A 状态。
影响因子：
2.9
作者：
Marmorino,JL;Pielak,GJ
通讯作者：
Pielak,GJ
影响因子：
56.9
作者：
JENNINGS, PA;WRIGHT, PE
通讯作者：
WRIGHT, PE
来自 Caudina arenicola 的单体半色素和二聚氰基血红蛋白的结构分析。
影响因子：
5.6
作者：
Mitchell,DT;Kitto,GB;Hackert,ML
通讯作者：
Hackert,ML
2.5 A 分辨率下 Urechis caupo 的同源四聚体血红蛋白的结构测定和精化。
DOI：
10.1107/s0108768191012363
发表时间：
1992
期刊：
Acta crystallographica. Section B, Structural science
影响因子：
--
作者：
Kolatkar,PR;Ernst,SR;Hackert,ML;Ogata,CM;Hendrickson,WA;Merritt,EA;Phizackerley,RP
通讯作者：
Phizackerley,RP
影响因子：
56.9
作者：
HUGHSON, FM;WRIGHT, PE;BALDWIN, RL
通讯作者：
BALDWIN, RL