M. V. Petoukhov, T. V. Rakitina, Yu. K. Agapova, D. E. Petrenko, P. V. Konarev, V. V. Britikov, E. V. Britikova, E. V. Bocharov, E. V. Shtykova
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引用次数: 0
摘要
摘要核团相关蛋白(NAPs)控制着细菌核团的结构和功能。组蛋白样 HU 蛋白是分裂细菌细胞中最丰富的 NAPs。此前,我们利用核磁共振光谱法获得了致病性支原体梅螺浆菌和五倍子支原体的 HU 蛋白构象的结构组合。通过小角 X 射线散射(SAXS)对这些支原体蛋白进行了结构研究。从 HU 蛋白质溶液的散射数据中估算出通过核磁共振获得的组合中个别构象的发生率。特别是,采用了一种基于平衡混合物各组分体积分数的表征方法。蛋白质的一般形状及其低聚状态通过ab initio珠子建模得到了独立证实。该方法基于将拟合 SAXS 数据的构象结构特征与这些特征在随机生成的集合中的分布进行比较。所获得的结果使人们对 HU 蛋白结构的可变性有了新的认识,而这种可变性是 HU 蛋白发挥作用的必要条件。
Comparative Structural Investigation of Histone-Like HU Proteins by Small-Angle X-ray Scattering
Abstract
Nucleoid-associated proteins (NAPs) control the structure and functions of bacterial nucleoid. Histone-like HU proteins are most abundant NAPs in dividing bacterial cells. Previously, structural ensembles of conformations of HU proteins from pathogenic mycoplasmas Spiroplasma melliferum and Mycoplasma gallisepticum were obtained using NMR spectroscopy. A structural study of these mycoplasma proteins is performed by small-angle X-ray scattering (SAXS). The occurrence of individual conformations from the ensemble, obtained by NMR, is estimated from the scattering data on HU protein solutions. In particular, an approach based on characterization of equilibrium mixtures in terms of volume fractions of their components was applied. The general shape of the proteins and their oligomeric state are independently confirmed using ab initio bead modelling. The flexibility of DNA-binding protein domains is analyzed by the ensemble optimization method, which is based on comparison of the structural characteristics of conformations fitting the SAXS data to the distribution of these characteristics in a randomly generated set. The results obtained give a new insight on the variability of the structure of HU proteins, which is necessary for their functioning.
期刊介绍:
Crystallography Reports is a journal that publishes original articles short communications, and reviews on various aspects of crystallography: diffraction and scattering of X-rays, electrons, and neutrons, determination of crystal structure of inorganic and organic substances, including proteins and other biological substances; UV-VIS and IR spectroscopy; growth, imperfect structure and physical properties of crystals; thin films, liquid crystals, nanomaterials, partially disordered systems, and the methods of studies.