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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structural and functional relationships in the hybrid cluster protein family: structure of the anaerobically purified hybrid cluster protein from Desulfovibrio vulgaris at 1.35 angstrom resolution
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Structural and functional relationships in the hybrid cluster protein family: structure of the anaerobically purified hybrid cluster protein from Desulfovibrio vulgaris at 1.35 angstrom resolution

机译：结构和功能的关系混合集群蛋白质家族:结构厌氧净化混合集群蛋白质从脱磷孤菌属寻常的为1.35埃决议

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摘要

The hybrid cluster protein (HCP) from the sulfate-reducing bacterium Desulfovibrio vulgaris strain Hildenborough has been isolated and crystallized anaerobically. The phase problem was solved for a P2(1)2(1)2(1) crystal form using multiple-wavelength anomalous diffraction data collected in the vicinity of the Fe K absorption edge. Although the overall protein structure is essentially the same as that previously obtained, it shows that the nature of the hybrid cluster has particular differences when isolated and crystallized in the absence of oxygen and this provides insight into the structural features associated with changes in the oxidation state. A comparison between HCPs and carbon monoxide dehydrogenases (CoDs) shows that they possess a similar fold and that the dehydrogenases have a related cluster at the equivalent HCP hybrid cluster position. This helps to understand the nature of the hybrid cluster and to predict a dimeric structure for class 3 HCPs, which lack the N-terminal region.
机译：混合集群蛋白质(HCP)硫酸盐还原细菌脱磷孤菌属寻常的应变Hildenborough孤立和结晶厌氧。解决了P2(1) 2(1) 2(1)晶体形式使用多波长反常衍射数据收集附近的铁K吸收边缘。本质上是一样的,以前,这表明混合集群的本质当孤立和有特别的差异呢结晶,这在缺乏氧气提供深入的结构特点与氧化态的变化有关。比较学校和一氧化碳脱氢酶(鳕科鱼)表明他们拥有相似的褶皱和脱氢酶有一个相关的等效HCP混合集群集群的位置。混合集群和预测的性质二聚的结构3班的学校,这所缺乏的氨基地区。

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