Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme
Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme
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DOI：
10.1093/emboj/17.14.4101
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发表时间：
1998-07-15
期刊：
影响因子：
11.4
通讯作者：
Steitz, TA
中科院分区：
文献类型：
--
作者：
Jeruzalmi, D;Steitz, TA
T7 RNA聚合酶-T7溶菌酶复合物在大肠杆菌感染期间调节噬菌体基因表达。该复合物的2.8埃晶体结构揭示了溶菌酶在远离聚合酶活性位点的位点结合，这表明了间接的抑制机制。T7 RNA聚合酶结构与DNA聚合酶的同源pol I家族的结构的比较揭示了催化位点的同一性，但也揭示了RNA聚合酶功能的特异性差异。这里提出的T7 RNA聚合酶的结构与以前发表的结构显著不同。噬菌体RNA聚合酶和那些从线粒体和叶绿体之间的序列相似性，在我们的T7 RNA聚合酶的修订模型的上下文中解释时，建议一个保守的倍。
The T7 RNA polymerase-T7 lysozyme complex regulates phage gene expression during infection of Escherichia coli. The 2.8 Angstrom crystal structure of the complex reveals that lysozyme binds at a site remote from the polymerase active site, suggesting an indirect mechanism of inhibition, Comparison of the T7 RNA polymerase structure with that of the homologous pol I family of DNA polymerases reveals identities in the catalytic site but also differences specific to RNA polymerase function. The structure of T7 RNA polymerase presented here differs significantly from a previously published structure. Sequence similarities between phage RNA polymerases and those from mitochondria and chloroplasts, when interpreted in the context of our revised model of T7 RNA polymerase, suggest a conserved fold.