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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Flexibility of the Cu,Zn superoxide dismutase structure investigated at 0.57 GPa.
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Flexibility of the Cu,Zn superoxide dismutase structure investigated at 0.57 GPa.

机译：灵活性的铜、锌超氧化物歧化酶结构调查0.57绩点。

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摘要

The 2 A resolution crystal structure of bovine erythrocyte Cu,Zn superoxide dismutase (CuZnSOD) has been determined by X-ray diffraction at high pressure (0.57 GPa) and room temperature. At 0.57 GPa the secondary, tertiary and quaternary structures are similar to other previously determined bovine erythrocyte CuZnSOD structures. Nevertheless, pressure has a localized impact on the atomic coordinates of C(alpha) atoms and on side chains. The compression of the crystal and of the protein backbone is anisotropic. This anisotropy is discussed, taking into account intermolecular contacts and protein conformation. Pressure perturbation highlights the more flexible zones in the protein such as the electrostatic loop. At 0.57 GPa, a global shift of the dimetallic sites in both subunits and changes in the oxidation state of Cu were observed. The flexibility of the electrostatic loop may be useful for the interaction of different metal carriers in the copper-uptake process, whereas the flexibility of the metal sites involved in the activity of the protein could contribute to explaining the ubiquitous character of CuZnSODs, which are found in organisms living in very different conditions, including the deep-sea environment. This work illustrates the potential of combining X-ray crystallography with high pressure to promote and stabilize higher energy conformational substates.
机译：2牛的分辨率晶体结构红细胞铜、锌超氧化物歧化酶(CuZnSOD)已经由x射线衍射在高吗压力(0.57 GPa)和室温。GPa二级、三级和四级结构类似于其他牛红细胞CuZnSOD结构决定的。然而,压力有局限性的影响C(α)原子的原子坐标侧链。蛋白质的支柱是各向异性。讨论了各向异性,考虑分子间的接触和蛋白质构象。压力扰动突显出更多灵活的区域在蛋白质等静电环。的子单元和dimetallic网站铜的氧化态的变化观察到。循环的相互作用可能是有用的不同的金属在copper-uptake运营商过程,而金属的灵活性网站参与蛋白质的活动可能有助于解释无处不在的CuZnSODs的性格,被发现生物生活在不同条件下,包括深海环境。说明了结合x射线的潜力结晶学与促进和高压高能量稳定构象亚态。

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