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首页> 外文期刊>Biochemistry >Crystal Structure and Solution NMR Dynamics of a D (Type II) Peroxiredoxin Glutaredoxin and Thioredoxin Dependent: A New Insight into the Peroxiredoxin Oligomerism.
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Crystal Structure and Solution NMR Dynamics of a D (Type II) Peroxiredoxin Glutaredoxin and Thioredoxin Dependent: A New Insight into the Peroxiredoxin Oligomerism.

机译：D（II型）过氧化物酶Glutaredoxin和硫氧还蛋白依赖性的晶体结构和溶液NMR动力学：对Peroxiredoxin齐聚物的新见解。

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摘要

Peroxiredoxins (Prxs) constitute a family of thiol peroxidases that reduce hydrogen peroxide, peroxinitrite, and hydroperoxides using a strictly conserved cysteine. Very abundant in all organisms, Prxs are produced as diverse isoforms characterized by different catalytic mechanisms and various thiol-containing reducing agents. The oligomeric state of Prxs and the link with their functionality is a subject of intensive research. We present here a combined X-ray and nuclear magnetic resonance (NMR) study of a plant Prx that belongs to the D-Prx (type II) subfamily. The Populus trichocarpa Prx is the first Prx shown to be regenerated in vitro by both the glutaredoxin and thioredoxin systems. The crystal structure and solution NMR provide evidence that the reduced protein is a specific noncovalent homodimer both in the crystal and in solution. The dimer interface is roughly perpendicular to the plane of the central betasheet and differs from the interface of A- and B-Prx dimers, where proteins associate inthe plane parallel to the beta sheet. The homodimer interface involves residues strongly conserved in the D (type II) Prxs, suggesting that all Prxs of this family can homodimerize. The study provides a new insight into the Prx oligomerism and the basis for protein-protein and enzyme-substrate interaction studies by NMR.
机译：过氧化物氧还蛋白（Prxs）构成了巯基过氧化物酶家族，可使用严格保留的半胱氨酸来还原过氧化氢，过氧化物亚硝酸盐和氢过氧化物。在所有生物中都非常丰富，Prxs以各种异构体形式产生，其特征在于不同的催化机理和各种含硫醇的还原剂。 Prxs的低聚状态及其功能的链接是深入研究的主题。我们在这里提出了属于D-Prx（II型）亚科的植物Prx的组合X射线和核磁共振（NMR）研究。毛果杨Prx是第一个显示出可通过戊二醛和硫氧还蛋白系统在体外再生的Prx。晶体结构和溶液NMR提供了证据，表明还原的蛋白质在晶体和溶液中都是特定的非共价同二聚体。二聚体界面大致垂直于中央βsheet的平面，并且不同于A-和B-Prx二聚体的界面，在A-和B-Prx二聚体中，蛋白质在平行于beta平面的平面内缔合。同型二聚体界面涉及在D（II型）Prxs中高度保守的残基，这表明该家族的所有Prxs都可以同型二聚体。该研究为Prx寡聚提供了新的见识，并为通过NMR进行蛋白质-蛋白质和酶-底物相互作用研究提供了基础。

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