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首页> 外文期刊>Journal of Molecular Biology >Non-functional conserved residues in globins and their possible role as a folding nucleus.
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Non-functional conserved residues in globins and their possible role as a folding nucleus.

机译：珠蛋白中的非功能性保守残基及其作为折叠核的可能作用。

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摘要

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.
机译：728个不同球蛋白亚家族的序列的基于结构的序列比对表明，在每个亚家族中，共有两个簇，其共有两个保守的残基。第一个是众所周知的“功能”簇，其中包括六个血红素结合的保守残基（Phe CD1，His F8;脂族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），它们不结合血红素但属于其直接邻域。此处显示的第二个簇（脂族A8，G16，G12;芳族A12;疏水性H8，可能还有H12）与血红素相距较远。它完全是非极性的，并且从每个螺旋A，G和H旋转一圈（i，i + 4位置）。已知在apomyoglobin折叠的最早阶段形成的A，G和H螺旋相对保持在平衡熔融小球状态下稳定，并且在此状态下可能彼此紧密堆积。我们已经证明在c型细胞色素中存在两个相似的保守簇，即血红素结合和血红素远端。 c细胞色素中的第二个簇包括N末端和C末端的α螺旋中的每一个螺旋。细胞色素c中的这些N和C末端螺旋是在蛋白质折叠的最早阶段形成的，在熔融小球状态下保持相对稳定，并且在此状态下彼此紧密堆积，类似于所观察到的球蛋白的行为。至少这两个大蛋白家族（c型细胞色素和球蛋白）在非功能性保守残基的存在和相互位置上具有相似的相似性。我们假设非功能性保守残基是将这两个蛋白家族快速正确折叠到其稳定3D结构中所必需的。

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