转录终止因子rho的RNA结合结构域的晶体结构
Crystal structure of the RNA-binding domain from transcription termination factor rho.
作者信息
Allison T J, Wood T C, Briercheck D M, Rastinejad F, Richardson J P, Rule G S
出版信息
Nat Struct Biol. 1998 May;5(5):352-6. doi: 10.1038/nsb0598-352.
Transcription termination factor rho is an ATP-dependent hexameric helicase found in most eubacterial species. The Escherichia coli rho monomer consists of two domains, an RNA-binding domain (residues 1-130) and an ATPase domain (residues 131-419). The ATPase domain is homologous to the beta subunit of F1-ATPase. Here, we report that the crystal structure of the RNA-binding domain of rho (rho130) at 1.55 A confirms that rho130 contains the oligosaccharide/oligonucleotide-binding (OB) fold, a five stranded beta-barrel. The beta-barrel of rho130 is also surprisingly similar to the N-terminal beta-barrel of F1 ATPase, extending the applicability of F1 ATPase as a structural model for hexameric rho.
转录终止因子ρ是一种ATP依赖的六聚体解旋酶，存在于大多数真细菌物种中。大肠杆菌的ρ单体由两个结构域组成，一个RNA结合结构域（第1至130位氨基酸残基）和一个ATP酶结构域（第131至419位氨基酸残基）。该ATP酶结构域与F1-ATP酶的β亚基同源。在此，我们报告ρ的RNA结合结构域（ρ130）在1.55 Å分辨率下的晶体结构，证实ρ130含有寡糖/寡核苷酸结合（OB）折叠，即一个五链β桶结构。ρ130的β桶结构也惊人地类似于F1 ATP酶的N端β桶结构，这扩展了F1 ATP酶作为六聚体ρ的结构模型的适用性。
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