DNA RECOGNITION BY BETA-SHEETS IN THE ARC REPRESSOR-OPERATOR CRYSTAL-STRUCTURE
DNA RECOGNITION BY BETA-SHEETS IN THE ARC REPRESSOR-OPERATOR CRYSTAL-STRUCTURE
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DOI：
10.1038/367754a0
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发表时间：
1994-02-24
期刊：
影响因子：
64.8
通讯作者：
SAUER, RT
中科院分区：
文献类型：
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作者：
RAUMANN, BE;ROULD, MA;SAUER, RT
在噬菌体P22裂解生长期间，ant基因的转录（参考文献1）受两个Arc阻遏物二聚体与21个碱基对操纵位点的协同结合调节2，3。在这里，我们报告的共晶结构的弧四聚体运营商复杂的2.6埃的分辨率。正如遗传学4 -6和结构研究7以及同源大肠杆菌MetJ阻遏物8的共晶体结构所预期的那样，每个Arc二聚体使用反平行β折叠来识别大沟中的碱基。然而，Arc和MetJ复合物在几个重要方面有所不同：Arc的β-折叠-DNA相互作用远不对称; Arc与DNA的结合伴随着β-折叠的重要构象变化; Arc使用其蛋白质表面的不同部分进行二聚体-二聚体相互作用。
TRANSCRIPTION of the ant gene during lytic growth of bacteriophage P22 (ref. 1) is regulated by the cooperative binding of two Arc repressor dimers to a 21-base-pair operator site2,3. Here we report the co-crystal structure of this Arc tetramer-operator complex at 2.6 angstrom resolution. As expected from genetic4-6 and structural studies7 and from the co-crystal structure of the homologous Escherichia coli MetJ repressor8, each Arc dimer uses an antiparallel beta-sheet to recognize bases in the major groove. However, the Arc and MetJ complexes differ in several important ways: the beta-sheet-DNA interactions of Arc are far less symmetrical; DNA binding by Arc is accompanied by important conformational changes in the beta-sheet; and Arc uses a different part of its protein surface for dimer-dimer interactions.