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首页> 美国卫生研究院文献>Protein Science : A Publication of the Protein Society >Comparison of the crystal structures of genetically engineered human manganese superoxide dismutase and manganese superoxide dismutase from Thermus thermophilus: differences in dimer-dimer interaction.
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Comparison of the crystal structures of genetically engineered human manganese superoxide dismutase and manganese superoxide dismutase from Thermus thermophilus: differences in dimer-dimer interaction.

机译：转基因人类锰超氧化物歧化酶和嗜热栖热菌锰超氧化物歧化酶的晶体结构比较：二聚体-二聚体相互作用的差异。

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摘要

The three-dimensional X-ray structure of a recombinant human mitochondrial manganese superoxide dismutase (MnSOD) (chain length 198 residues) was determined by the method of molecular replacement using the related structure of MnSOD from Thermus thermophilus as a search model. This tetrameric human MnSOD crystallizes in space group P2(1)2(1)2 with a dimer in the asymmetric unit (Wagner, U.G., Werber, M.M., Beck, Y., Hartman, J.R., Frolow, F., & Sussman, J.L., 1989, J. Mol. Biol. 206, 787-788). Refinement of the protein structure (3,148 atoms with Mn and no solvents), with restraints maintaining noncrystallographic symmetry, converged at an R-factor of 0.207 using all data from 8.0 to 3.2 A resolution and group thermal parameters. The monomer-monomer interactions typical of bacterial Fe- and Mn-containing SODs are retained in the human enzyme, but the dimer-dimer interactions that form the tetramer are very different from those found in the structure of MnSOD from T. thermophilus. In human MnSOD one of the dimers is rotated by 84 degrees relative to its equivalent in the thermophile enzyme. As a result the monomers are arranged in an approximately tetrahedral array, the dimer-dimer packing is more intimate than observed in the bacterial MnSOD from T. thermophilus, and the dimers interdigitate. The metal-ligand interactions, determined by refinement and verified by computation of omit maps, are identical to those observed in T. thermophilus MnSOD.
机译：重组人线粒体锰超氧化物歧化酶（MnSOD）的三维X射线结构（链长198个残基）使用嗜热栖热菌的MnSOD的相关结构作为搜索模型，通过分子置换的方法确定。这种四聚体MnSOD在空间群P2（1）2（1）2中以不对称单元中的二聚体（Wagner，UG，Werber，MM，Beck，Y.，Hartman，JR，Frolow，F。和Sussman， JL，1989，分子生物学杂志206，787-788）。使用从8.0 A到3.2 A分辨率的所有数据和组热参数，通过保持非晶体对称性的约束，精制蛋白质结构（3,148个含Mn和无溶剂的原子），使其收敛于R系数为0.207。典型的细菌含铁和含锰超氧化物歧化酶的单体-单体相互作用保留在人酶中，但形成四聚体的二聚体-二聚体相互作用与嗜热链球菌MnSOD的结构存在很大差异。在人类MnSOD中，其中一个二聚体相对于嗜热酶中的二聚体旋转了84度。结果，单体排列成近似四面体的阵列，二聚体-二聚体的堆积比嗜热链球菌的细菌MnSOD更为紧密，二聚体相互交叉。通过精炼确定并通过忽略图的计算验证的金属-配体相互作用与嗜热链球菌MnSOD中观察到的相同。

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