CRYSTALLOGRAPHIC STUDY OF T7 DNA POLYMERASE W/ DNA PRIMER TEMPLATE & NUCLEOTIDES

目前的生化和结构数据表明，DNA 来自各种生物体的聚合酶使用类似的催化 DNA合成的机制。更准确地理解 这些蛋白质的反应机理及对它们的鉴定 决定其底物专一性的结构特征， 加工性和其他酶性质有待高分辨率 催化活性络合物中DNA聚合酶的结构 以DNA和核苷酸为底物。现有的DNA聚合酶 结构仅限于适应于分布的酶 短间隙合成和，除了一个例外(POL P)，这些结构 缺少一个或两个底物。我们正在调查 T7DNA聚合酶的结构及其与底物的相互作用 它与DNA复制叉的其他蛋白质的关系 很复杂。

Current biochemical and structural data suggest that DNA polymerases from a variety of organisms use similar catalytic mechanisms for the synthesis of DNA. A more precise understanding of the reaction mechanisms of these proteins and the identification of structural features that dictate their substrate specificity, processivity, and other enzymatic properties await high resolution structures of DNA polymerases in catalytically-competent complexes with DNA and nucleotide substrates. The existing DNA polymerase structures are limited to enzymes that are adapted for distributive short-gap synthesis and, with one exception (Pol P), these structures are missing one or both substrates. We are investigating the structure of T7 DNA polymerase, its interaction with substrates, and its association with other proteins of the DNA replication fork complex.