Protein stability indicates divergent evolution of PD-(D/E)XK type II restriction endonucleases.

ABSTRACT: Type II restriction endonucleases recognize 4-8 base-pair-long DNA sequences and catalyze their cleavage with remarkable specificity. Crystal structures of the PD-(DE)XK superfamily revealed a common alpha/beta core motif and similar active site. In contrast, these enzymes show little sequence similarity and use different strategies to interact with their substrate DNA. The intriguing question is whether this enzyme family could have evolved from a common origin. In our present work, protein structure stability elements were analyzed and compared in three parts of PD-(DE)XK type II restriction endonucleases: (1) core motif, (2) active-site residues, and (3) residues playing role in DNA recognition. High correlation was found between the active-site residues and those stabilization factors

SUBMITTER: Fuxreiter M 

PROVIDER: S-EPMC2373676 | biostudies-literature | 2002 Aug

REPOSITORIES: biostudies-literature