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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structure Of Polc Reveals Unique Dna Binding And Fidelity Determinants
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Structure Of Polc Reveals Unique Dna Binding And Fidelity Determinants

机译：Polc的结构揭示了独特的Dna结合和保真决定因素

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摘要

PolC is the polymerase responsible for genome duplication in many Gram-positive bacteria and represents an attractive target for antibacterial development. We have determined the 2.4-A resolution crystal structure of Geobacillus kaustophilus PolC in a ternary complex with DNA and dGTP. The structure reveals nascent base pair interactions that lead to highly accurate nucleotide incorporation. A unique β-strand motif in the PolC thumb domain contacts the minor groove, allowing replication errors to be sensed up to 8 nt upstream of the active site. PolC exhibits the potential for large-scale conformational flexibility, which could encompass the catalytic residues. The structure suggests a mechanism by which the active site can communicate with the rest of the replisome to trigger proofreading after nucleotide misincorporation, leading to an integrated model for controlling the dynamic switch between replicative and repair polymerases. This ternary complex of a cellular replicative polymerase affords insights into polymerase fidelity, evolution, and structural diversity.
机译：PolC是负责在许多革兰氏阳性细菌中进行基因组复制的聚合酶，是抗菌发展的诱人靶标。我们确定了带有DNA和dGTP的三元复合物中的嗜碱芽孢杆菌PolC的2.4-A分辨率晶体结构。该结构揭示了新生的碱基对相互作用，可导致高度精确的核苷酸掺入。 PolC拇指域中独特的β链基序与小沟接触，从而可在活性位点上游最多8 nt处检测到复制错误。 PolC具有潜在的大规模构象柔韧性，可能包含催化残基。该结构表明了一种机制，通过该机制，活性位点可以与核苷酸复制子掺入后的其余复制体进行通讯，从而触发校对，从而形成了一个用于控制复制和修复聚合酶之间动态切换的整合模型。细胞复制性聚合酶的三元复合物提供了对聚合酶保真度，进化和结构多样性的见解。

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