Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics.
Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics.
复制标题
DOI：
10.1007/s12104-015-9637-8
复制
发表时间：
2016-04
影响因子：
0.9
通讯作者：
Karplus PA
中科院分区：
文献类型：
--
作者：
Buchko GW;Perkins A;Parsonage D;Poole LB;Karplus PA
过氧化还原蛋白 (Prx) 是一种普遍存在的酶，可减少过氧化物，作为抗氧化防御和氧化还原信号传导的一部分。虽然 Prx 催化活性和对过氧化失活的敏感性取决于它们的动态特性，但很少有例子可以通过 NMR 光谱来表征它们的动态。在这里，我们通过指定还原态（二硫醇）和氧化态（二硫化物）的可观察到的 1HN、15N、13Cα、13Cβ 和 13C' 化学位移，为研究植物病原体黄单胞菌 (XcPrxQ) 的过氧化还原蛋白 Q 的溶液特性奠定了基础。在还原态下，大部分主链酰胺共振 (149/152, 98%) 可以归属于 XcPrxQ 1H-15N HSQC 谱。相比之下，这些酰胺共振中有 51% (77) 在酶二硫键状态的 1H-15N HSQC 谱中不可见，表明与分子内 C48-C84 二硫键形成相关的主链动力学发生了显着变化。
Peroxiredoxins (Prx) are ubiquitous enzymes that reduce peroxides as part of antioxidant defenses and redox signaling. While Prx catalytic activity and sensitivity to hyperoxidative inactivation depend on their dynamic properties, there are few examples where their dynamics has been characterized by NMR spectroscopy. Here, we provide a foundation for studies of the solution properties of peroxiredoxin Q from the plant pathogen Xanthomonas campestris (XcPrxQ) by assigning the observable 1HN, 15N, 13Cα, 13Cβ, and 13C′ chemical shifts for both the reduced (dithiol) and oxidized (disulfide) states. In the reduced state, most of the backbone amide resonances (149/152, 98%) can be assigned in the XcPrxQ 1H-15N HSQC spectrum. In contrast, a remarkable 51% (77) of these amide resonances are not visible in the 1H-15N HSQC spectrum of the disulfide state of the enzyme, indicating a substantial change in backbone dynamics associated with the formation of an intramolecular C48-C84 disulfide bond.