Vos Werner L, Nazarov Petr V, Koehorst Rob B M, Spruijt Ruud B, Hemminga Marcus A
Department of Biology, National University of Ireland Maynooth, County Kildare, Ireland.
Trends Biochem Sci. 2009 May;34(5):249-55. doi: 10.1016/j.tibs.2009.01.007. Epub 2009 Apr 8.
The major coat protein of the filamentous bacteriophage M13 is a surprising protein because it exists both as a membrane protein and as part of the M13 phage coat during its life cycle. Early studies showed that the phage-bound structure of the coat protein was a continuous I-shaped alpha-helix. However, throughout the years various structural models, both I-shaped and L-shaped, have been proposed for the membrane-bound state of the coat protein. Recently, site-directed labelling approaches have enabled the study of the coat protein under conditions that more closely mimic the in vivo membrane-bound state. Interestingly, the structure that has emerged from this work is I-shaped and similar to the structure in the phage-bound state.
丝状噬菌体M13的主要外壳蛋白是一种令人惊讶的蛋白质,因为在其生命周期中,它既作为膜蛋白存在,又作为M13噬菌体外壳的一部分存在。早期研究表明,外壳蛋白的噬菌体结合结构是连续的I形α螺旋。然而,多年来,针对外壳蛋白的膜结合状态提出了各种结构模型,包括I形和L形。最近,定点标记方法使得能够在更接近模拟体内膜结合状态的条件下研究外壳蛋白。有趣的是,这项研究得出的结构是I形的,与噬菌体结合状态下的结构相似。