Chang Caleb, Zhou Grace, Gao Yang
Department of Biosciences, Rice University, Houston, Texas 77005, USA.
Struct Dyn. 2023 Jun 15;10(3):034702. doi: 10.1063/4.0000187. eCollection 2023 May.
DNA polymerases are the enzymatic catalysts that synthesize DNA during DNA replication and repair. Kinetic studies and x-ray crystallography have uncovered the overall kinetic pathway and led to a two-metal-ion dependent catalytic mechanism. Diffusion-based time-resolved crystallography has permitted the visualization of the catalytic reaction at atomic resolution and made it possible to capture transient events and metal ion binding that have eluded static polymerase structures. This review discusses past static structures and recent time-resolved structures that emphasize the crucial importance of primer alignment and different metal ions binding during catalysis and substrate discrimination.
DNA聚合酶是在DNA复制和修复过程中合成DNA的酶促催化剂。动力学研究和X射线晶体学揭示了整体动力学途径，并得出了一种双金属离子依赖性催化机制。基于扩散的时间分辨晶体学使得在原子分辨率下可视化催化反应成为可能，并且能够捕捉到静态聚合酶结构所无法揭示的瞬态事件和金属离子结合情况。本综述讨论了过去的静态结构和最近的时间分辨结构，这些结构强调了引物排列以及催化和底物识别过程中不同金属离子结合的至关重要性。
