大肠杆菌应激蛋白YciF的晶体结构。
The crystal structure of the E. coli stress protein YciF.
作者信息
Hindupur Aditya, Liu Deqian, Zhao Yonghong, Bellamy Henry D, White Mark A, Fox Robert O
机构信息
Department of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, Texas 77555-0647, USA.
出版信息
Protein Sci. 2006 Nov;15(11):2605-11. doi: 10.1110/ps.062307706. Epub 2006 Sep 25.
Abstract
YciF is a protein that is up-regulated when bacteria experience stress conditions, and is highly conserved in a range of bacterial species. YciF has no known structure or biochemical function. To learn more about its potential molecular function and its role in the bacterial stress response, we solved the crystal structure of YciF at 2.0 Angstrom resolution by the multiple wavelength anomalous diffraction (MAD) technique. YciF is a dimer in solution, and forms a homodimer in the crystal asymmetric unit. The two monomers form a dimer with a molecular twofold axis, with a significant burial of solvent-accessible surface area. The protein is an all-alpha protein composed of five helices: a four-helix bundle, and a short additional helix at the dimer interface. The protein is structurally similar to portions of the diiron-containing proteins, rubrerythrin and the Bacillus anthracis Dlp-2.
摘要
YciF是一种在细菌经历应激条件时上调的蛋白质，并且在一系列细菌物种中高度保守。YciF的结构或生化功能尚不清楚。为了更多地了解其潜在的分子功能及其在细菌应激反应中的作用，我们通过多波长反常衍射（MAD）技术以2.0埃的分辨率解析了YciF的晶体结构。YciF在溶液中是二聚体，在晶体不对称单元中形成同型二聚体。两个单体形成具有分子二重轴的二聚体，溶剂可及表面积有显著埋藏。该蛋白质是一种全α蛋白质，由五个螺旋组成：一个四螺旋束，以及在二聚体界面处的一个短的附加螺旋。该蛋白质在结构上与含铁二聚体蛋白质、红藓红素和炭疽芽孢杆菌Dlp-2的部分相似。
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