Venclovas C, Timinskas A, Siksnys V
Institute of Biotechnology Fermentas, Vilnius, Lithuania.
Proteins. 1994 Nov;20(3):279-82. doi: 10.1002/prot.340200308.
Examination of crystal structures of restriction endonucleases EcoRI and EcoRV complexes with their cognate DNA revealed a common structural element, which forms the core of both proteins. This element consists of a five-stranded beta-sheet and two alpha-helices packed against it and could be described as alpha-beta sandwich in which helices and beta-strands lie in two stacked layers. While the spatial structure of this alpha-beta sandwich is conserved in both enzymes, there are not detectable similarities between amino acid sequences except of a few residues involved in active site formation. Probably, other restriction endonucleases which have similar organization of the active site might possess similar structural element regardless of DNA sequence recognized and recognition elements in the enzyme used.
对限制性内切酶EcoRI和EcoRV与其同源DNA形成的复合物的晶体结构进行研究后发现了一个共同的结构元件,它构成了这两种蛋白质的核心。该元件由一个五链β折叠和与之堆积的两个α螺旋组成,可以描述为α-β三明治结构,其中螺旋和β链位于两个堆叠层中。虽然这种α-β三明治的空间结构在两种酶中都是保守的,但除了少数参与活性位点形成的残基外,氨基酸序列之间没有可检测到的相似性。可能,其他具有相似活性位点组织的限制性内切酶可能具有相似的结构元件,而不管所识别的DNA序列和所用酶中的识别元件如何。