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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of cyclized green fluorescent protein.
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Structure of cyclized green fluorescent protein.

机译：环化绿色荧光蛋白的结构。

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摘要

Crystals of cyclic green fluorescent protein (cGFP) engineered by the previously reported split intein technology [Iwai et al. (2001), J. Biol. Chem. 276, 16548-16554] were obtained and the structure was solved using molecular replacement. Although the core of the protein can unambiguously be fitted from the first to the last residue of the genuine sequence, the electron density in the region of the linker peptide is rather poor owing to the high water content of the crystals. Therefore, it is concluded that this part of the protein is highly disordered in the present structure and is very flexible. This is supported by the absence of crystal contacts in the linker-peptide region and the fact that the core of the protein exhibits a very similar conformation to that known from other GFP structures, thereby not implicating any constraints arising from the presence of the artificial linker. Nevertheless, the density is consistent with the loop being intact, as confirmed by mass spectroscopy of dissolved crystals. The present structure contains an antiparallel cGFP dimer where the dimer interface is clearly different from other crystal structures featuring two GFP molecules. This adds further support to the fact that the cylinder surface of GFP is rather versatile and can employ various polar and non-polar patches in protein-protein interactions.
机译：循环绿色荧光蛋白的晶体之前报道(cGFP)工程分裂intein技术[自制et al。(2001),J。医学杂志。使用分子结构解决了更换。从第一个明确地安装最后残留的真正的序列,链接器的电子密度在该地区肽是相当可怜的由于高水位晶体的内容。得出的结论是,这部分的蛋白质是高度无序的结构和非常灵活。水晶linker-peptide地区和联系人事实上,蛋白质的核心展品非常相似的已知的构象其他GFP结构,从而没有暗示约束的存在引起的人工链接器。被完好无损,符合循环经质谱分析的溶解晶体。反平行的cGFP二聚体,二聚体界面显然是不同于其他水晶吗有两个绿色荧光蛋白分子结构。进一步支持这一事实缸GFP表面相当多才多艺,可以使用在各种极性和非极性补丁蛋白质相互作用。

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