Crystal structure of the catalytic α subunit of E. coli replicative DNA polymerase III
Crystal structure of the catalytic α subunit of E. coli replicative DNA polymerase III
复制标题
DOI：
10.1016/j.cell.2006.07.028
复制
发表时间：
2006-09-08
期刊：
影响因子：
64.5
通讯作者：
Kuriyan, John
中科院分区：
文献类型：
--
作者：
Lamers, Meindert H.;Georgescu, Roxana E.;Kuriyan, John
细菌复制DNA聚合酶如聚合酶III(PolIII)与其他聚合酶没有序列相似性。在2.3埃分辨率下测定的Pol III大片段(残基1-917)的晶体结构显示了一个独特的链折叠，其催化结构域与DNA聚合酶β和相关的核苷酸转移酶具有局限性的相似性。POL III的结构与包括真核复制聚合酶在内的典型DNA聚合酶家族成员的结构显著不同，这表明细菌中的DNA复制机制是独立产生的。Pol III活性部位附近的一个结构元件，它不存在于核苷酸转移酶中，但与一些典型的DNA聚合酶活性部位的元件相似，这表明在更远的水平上，所有DNA聚合酶可能共享一个共同的祖先。该结构还提出了Pol III与滑动钳和DNA相互作用的模型。
Bacterial replicative DNA polymerases such as Polymerase III (Pol III) share no sequence similarity with other polymerases. The crystal structure, determined at 2.3 angstrom resolution, of a large fragment of Pol III (residues 1-917), reveals a unique chain fold with localized similarity in the catalytic domain to DNA polymerase beta and related nucleotidyltransferases. The structure of Pol III is strikingly different from those of members of the canonical DNA polymerase families, which include eukaryotic replicative polymerases, suggesting that the DNA replication machinery in bacteria arose independently. A structural element near the active site in Pol III that is not present in nucleotidyltransferases but which resembles an element at the active sites of some canonical DNA polymerases suggests that, at a more distant level, all DNA polymerases may share a common ancestor. The structure also suggests a model for interaction of Pol III with the sliding clamp and DNA.