Role of structural determinants in folding of the sandwich-like protein Pseudomonas aeruginosa azurin.
Role of structural determinants in folding of the sandwich-like protein Pseudomonas aeruginosa azurin.
复制标题
结构决定因素在三明治样蛋白铜绿假单胞菌天青蛋白折叠中的作用。
DOI：
10.1073/pnas.0501038102
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发表时间：
2005
期刊：
影响因子：
--
通讯作者：
Wittung-Stafshede,Pernilla
中科院分区：
文献类型：
--
作者：
Wilson,CoreyJ;Wittung-Stafshede,Pernilla
一个不变的亚结构，形成两个互锁对相邻的β-链发生在基本上所有已知的类β-蛋白质。这些链中的8个保守位置最近被证明是结构决定因素。为了测试在这些不变位置处的残基是否对于机制（即，折叠核的一部分）或高能的（即，出于天然状态稳定性）的原因，我们描述了八个点突变的类似蛋白质铜绿假单胞菌-天青蛋白变体的折叠行为。我们发现一个简单的保守位置之间的关系：一半的残基形成天然的折叠过渡态的相互作用，而其他人不参与折叠核，但管理高天然状态的稳定性。因此，这些特定位置的进化保存为类β-淀粉样蛋白家族的成员提供了机制和能量优势。
An invariant substructure that forms two interlocked pairs of neighboring β-strands occurs in essentially all known sandwich-like proteins. Eight conserved positions in these strands were recently shown to act as structural determinants. To test whether the residues at these invariant positions are conserved for mechanistic (i.e., part of folding nucleus) or energetic (i.e., governing native-state stability) reasons, we characterized the folding behavior of eight point-mutated variants of the sandwich-like proteinPseudomonas aeruginosaapo-azurin. We find a simple relationship among the conserved positions: half of the residues form native-like interactions in the folding transition state, whereas the others do not participate in the folding nucleus but govern high native-state stability. Thus, evolutionary preservation of these specific positions gives both mechanistic and energetic advantages to members of the sandwich-like protein family.