Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments
Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments
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DOI：
10.1016/j.febslet.2014.01.029
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发表时间：
2014-03-03
期刊：
影响因子：
3.5
通讯作者：
Loewe, Jan
中科院分区：
文献类型：
--
作者：
Izore, Thierry;Duman, Ramona;Loewe, Jan
肌动蛋白家族的聚合蛋白几乎无处不在。Crenactin，仅限于Crenarchaea，比细菌MreB更接近肌动蛋白。Crenactins出现在基因簇中，暗示着一种未知但保守的功能。我们解决了crenactin的晶体结构在3.2埃分辨率。该蛋白质结晶为连续的右手螺旋，每一整圈有8个亚基，跨度为419埃。crenactin的结构显示了几个比肌动蛋白更长的环，但总体而言，crenactin与真核肌动蛋白密切相关，RMSD为1.6埃。通过电子显微镜成像的Crenactin细丝显示具有非常相似的螺旋参数的聚合物。(C)2014年欧洲生物化学学会联合会。Elsevier B.V.出版，保留所有权利。
Polymerising proteins of the actin family are nearly ubiquitous. Crenactins, restricted to Crenarchaea, are more closely related to actin than bacterial MreB. Crenactins occur in gene clusters hinting at an unknown, but conserved function. We solved the crystal structure of crenactin at 3.2 angstrom resolution. The protein crystallises as a continuous right-handed helix with 8 subunits per complete turn, spanning 419 angstrom. The structure of crenactin shows several loops that are longer than in actin, but overall, crenactin is closely related to eukaryotic actin, with an RMSD of 1.6 angstrom. Crenactin filaments imaged by electron microscopy showed polymers with very similar helical parameters. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.