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Structure of Arabidopsis chloroplastic monothiol glutaredoxin AtGRXcp.

机译:拟南芥叶绿素monothiol结构

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Monothiol glutaredoxins (Grxs) play important roles in maintaining redox homeostasis in living cells and are conserved across species. Arabidopsis thaliana monothiol glutaredoxin AtGRXcp is critical for protection from oxidative stress in chloroplasts. The crystal structure of AtGRXcp has been determined at 2.4 A resolution. AtGRXcp has a glutaredoxin/thioredoxin-like fold with distinct structural features that differ from those of dithiol Grxs. The structure reveals that the putative active-site motif CGFS is well defined and is located on the molecular surface and that a long groove extends to both sides of the catalytic Cys97. Structural comparison and molecular modeling suggest that glutathione can bind in this groove and form extensive interactions with conserved charged residues including Lys89, Arg126 and Asp152. Further comparative studies reveal that a unique loop with five additional residues adjacent to the active-site motif may be a key structural feature of monothiol Grxs and may influence their function. This study provides the first structural information on plant CGFS-type monothiol Grxs, allowing a better understanding of the redox-regulation mechanism mediated by these plant Grxs.
机译:Monothiol glutaredoxins (Grxs)扮演了一个重要的角色在维持氧化还原体内平衡的生活细胞和跨物种是守恒的。拟南芥monothiol glutaredoxinAtGRXcp氧化的保护是至关重要的压力在叶绿体。AtGRXcp已经确定在2.4一项决议。AtGRXcp glutaredoxin / thioredoxin-like褶皱不同的不同的结构特点的二硫酚Grxs。cgf是公认的活性部位图案定义和位于分子的表面,一个长槽两边延伸催化Cys97。分子建模表明,谷胱甘肽绑定在这个槽,形成广泛的与守恒的残留物包括Lys89 Arg126 Asp152。比较研究表明,一个独特的循环附近有5个额外的残留物活性位点的主题可能是一个关键的结构特征的monothiol Grxs并可能影响他们函数。植物CGFS-type结构信息monothiol Grxs,允许一个更好的理解redox-regulation机制介导的这些植物Grxs。

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