Janecek S
Department of Biochemical Technology, Faculty of Chemical Technology, Slovak Technical University, Bratislava, Czech and Slovak Federal Republic.
FEBS Lett. 1993 Jan 18;316(1):23-6. doi: 10.1016/0014-5793(93)81729-j.
The parallel (alpha/beta)8-barrel is a frequently occurring protein-folding motif. Although the arrangement of secondary structural elements along the barrel is very similar in different (alpha/beta)8-barrel enzymes, there is a very low mutual amino acid sequence homology among the enzymes, contributing in part to the hazy view of their evolution. Here an approach to identifying at least the rough of evolutionarily conserved (alpha/beta)8-barrel sequence is presented. Based on the idea that highly conserved sequence regions of a particular enzyme should be more or less conserved in the sequences of the other evolutionary related enzymes, five sequence similarities of ten different (alpha/beta)8-barrel enzymes were revealed, using the five conserved regions of the amino acid sequence of the alpha-amylase (alpha/beta)8-barrel as the templates.
平行(α/β)8桶状结构是一种常见的蛋白质折叠基序。尽管在不同的(α/β)8桶状酶中,沿桶状结构的二级结构元件排列非常相似,但这些酶之间的氨基酸序列同源性非常低,这在一定程度上导致了对它们进化的模糊认识。本文提出了一种方法,用于至少大致鉴定进化上保守的(α/β)8桶状序列。基于特定酶的高度保守序列区域在其他进化相关酶的序列中应或多或少保守的观点,以α-淀粉酶(α/β)8桶状结构氨基酸序列的五个保守区域为模板,揭示了十种不同(α/β)8桶状酶的五个序列相似性。