Crystal structure of a DNA-dependent RNA polymerase (DNA primase)
Crystal structure of a DNA-dependent RNA polymerase (DNA primase)
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DOI：
10.1038/83060
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发表时间：
2001-01-01
期刊：
影响因子：
--
通讯作者：
Kaiser, JT
中科院分区：
文献类型：
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作者：
Augustin, MA;Huber, R;Kaiser, JT
引物酶是每个生物体 DNA 复制装置的重要组成部分。它们催化单链 DNA 上寡核糖核苷酸的合成，随后充当复制 DNA 聚合酶的引物。与细菌引物酶相反，古细菌酶与其真核生物酶密切相关。我们通过多波长反常色散方法，以 2.3 埃的分辨率解析了超嗜热古菌激烈火球菌催化引物酶亚基的晶体结构。该结构显示出两个结构域的排列，其中一个新颖的锌指节基序位于引物酶 (prim) 结构域中。在古菌/真核引物酶家族的完整蛋白质的第一个结构中，催化活性残基的排列类似于折叠中不相关的各种DNA聚合酶的活性位点。
Primases are essential components of the DNA replication apparatus in every organism. They catalyze the synthesis of oligoribonucleotides on single-stranded DNA, which subsequently serve as primers for the replicative DNA polymerases. In contrast to bacterial primases, the archaeal enzymes are closely related to their eukaryotic counterparts. We have soh ed the crystal structure of the catalytic primase subunit from the hyperthermophilic archaeon Pyrococcus furiosus at 2.3 Angstrom resolution by multiwavelength anomalous dispersion methods. The structure shows a two-domain arrangement with a novel zinc knuckle motif located in the primase (prim) domain. In this first structure of a complete protein of the archael/eukaryotic primase family, the arrangement of the catalytically active residue resembles the active sites of various DNA polymerase that are unrelated in fold.