噬菌体λ O复制起始蛋白的起源结合结构域的结晶及初步晶体学表征
Crystallization and preliminary crystallographic characterization of the origin-binding domain of the bacteriophage lambda O replication initiator.
作者信息
Struble E B, Gittis A G, Bianchet M A, McMacken R
机构信息
Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt 6):542-5. doi: 10.1107/S1744309107022762. Epub 2007 May 31.
Abstract
The bacteriophage lambda O protein binds to the lambda replication origin (orilambda) and serves as the primary replication initiator for the viral genome. The binding energy derived from the binding of O to orilambda is thought to help drive DNA opening to facilitate initiation of DNA replication. Detailed understanding of this process is severely limited by the lack of high-resolution structures of O protein or of any lambdoid phage-encoded paralogs either with or without DNA. The production of crystals of the origin-binding domain of lambda O that diffract to 2.5 A is reported. Anomalous dispersion methods will be used to solve this structure.
摘要
噬菌体λ O蛋白与λ复制起点（oriλ）结合，作为病毒基因组的主要复制起始因子。O蛋白与oriλ结合产生的结合能被认为有助于推动DNA解链，促进DNA复制起始。由于缺乏O蛋白或任何λ样噬菌体编码的旁系同源物（无论有无DNA）的高分辨率结构，对这一过程的详细了解受到严重限制。本文报道了λ O蛋白的起源结合域晶体，其衍射分辨率达到2.5 Å。将使用反常散射方法来解析该结构。
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