Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-angstrom resolution
Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-angstrom resolution
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DOI：
10.1073/pnas.94.13.6652
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发表时间：
1997-06-24
影响因子：
11.1
通讯作者：
Waksman, G
中科院分区：
文献类型：
--
作者：
Raghunathan, S;Ricard, CS;Waksman, G
利用多波长异常色散在2.9埃的分辨率下测定了大肠杆菌单链DNA结合蛋白的四聚体DNA结合域的晶体结构，四聚体中的每个单体在拓扑结构上与寡聚体结合折叠相似。两个单体各贡献三条链到一个六链的单链上，形成二聚体。在晶体内观察到两个二聚体-二聚体界面，其中一个在溶液中稳定四聚体，另一个界面促进晶体内的超螺旋结构，该超螺旋结构反映了单链DNA结合蛋白与单链DNA的正合作结合中涉及的四聚体-四聚体相互作用。
The crystal structure of the tetrameric DNA-binding domain of the single-stranded DNA binding protein from Escherichia coli was determined at a resolution of 2.9 Angstrom using multiwavelength anomalous dispersion, Each monomer in the tetramer is topologically similar to an oligomer-binding fold. Two monomers each contribute three beta-strands to a single six-stranded beta-sheet to form a dimer. Two dimer-dimer interfaces are observed within the crystal, One of these stabilizes the tetramer in solution, The other interface promotes a superhelical structure within the crystal that mag reflect tetramer-tetramer interactions involved in the positive cooperative binding of the single-stranded DNA-binding protein to single-stranded DNA.