结构生物学sturcture biology explore-31.pdfVIP

? 2001 Nature Publishing Group review Comparative architecture of transposase and integrase complexes Phoebe A. Rice1 and Tania A. Baker2 Transposases and retroviral integrases promote the movement of DNA segments to new locations within and between genomes. These recombinases function as multimeric protein–DNA complexes. Recent success in solving the crystal structure of a Tn5 transposase–DNA complex provides the first detailed structural information about a member of the transposase/integrase superfamily in its active, DNA-bound state. Here, we summarize the reactions catalyzed by transposases and integrases and review the Tn5 transposase–DNA co- crystal structure. The insights gained from the Tn5 structure and other available structures are considered together with biochemical and genetic data to discuss features that are likely to prove common to the catalytic complexes used by members of this important protein family. Genes are supposed to stay in one place. However, cells carry pro- teins that are powerful antagonists of this founding principle of molecular biology. These are transposases that catalyze the move- ment of DNA segments, and the associated genes, to new DNA C sites. These proteins have dramatic biological and evolutionary consequences that shape the genomes of organisms. Remarkably, we have just learned that a full 45% of the DNA in the human N genome is transposable element-derived sequence1. Although RNase H there are several classes of transposition proteins, the best under- C stood are members of the transposase/retroviral integrase super-