Jäger J, Pata J D
School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.
Curr Opin Struct Biol. 1999 Feb;9(1):21-8. doi: 10.1016/s0959-440x(99)80004-9.
Underpinned by a database of more than a dozen different crystal structures, an increasingly complete and coherent picture of polymerase structure and function is emerging. Recently determined structures of DNA and RNA polymerases have revealed some of the molecular features and structural changes governing catalysis, oligomerization, processivity and fidelity. Despite having minimal similarities in sequence and protein topology, the polymerases all display a functionally analogous set of subdomains that bind the primer, template and nucleotide substrates in similar though not identical fashions. The two-metal-ion mechanism for nucleotide incorporation, however, is shared even by nonhomologous polymerases.
在一个包含十几种不同晶体结构的数据库的支撑下，关于聚合酶结构与功能的一幅越来越完整且连贯的图景正在浮现。最近确定的DNA和RNA聚合酶结构揭示了一些控制催化、寡聚化、持续合成能力和保真度的分子特征及结构变化。尽管在序列和蛋白质拓扑结构上相似度极低，但这些聚合酶都展示出一组功能类似的亚结构域，它们以相似但不完全相同的方式结合引物、模板和核苷酸底物。然而，核苷酸掺入的双金属离子机制甚至在非同源聚合酶中也是共有的。
