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首页> 外文期刊>Acta crystallographica.Section D Biological crystallography. >Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins
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Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins

机译：原子分辨率的晶体结构glutaredoxin 1和恶性疟原虫比较与其他glutaredoxins

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摘要

Glutaredoxins (Grxs) are redox proteins that use glutathione ( γGlu-Cys-Gly; GSH) as a cofactor. Plasmodium falciparum has one classic dithiol (CXXC) glutaredoxin (glutaredoxin 1; PfGrx1) and three monothiol (CXXS) Grx-like proteins (GLPs), which have five residue insertions prior to the active-site Cys. Here, the crystal structure of PfGrx1 has been determined by the sulfur single-wavelength anomalous diffraction (S-SAD) method utilizing intrinsic protein and solvent S atoms. Several residues were modelled with alternate conformations, and an alternate position was refined for the active-site Cys29 owing to radiation damage. The GSH-binding site is occupied by water polygons and buffer molecules. Structural comparison of PfGrx1 with other Grxs and Grx-like proteins revealed that the GSH-binding motifs (CXXC/CXXS, TVP, CDD, Lys26 and Gln/Arg63) are structurally conserved. Both the monothiol and dithiol Grxs possess three conserved water molecules; two of these were located in the GSH-binding site. PfGrx1 has several polar and charged amino-acid substitutions that provide structurally important additional hydrogen bonds and salt bridges missing in other Grxs.
机译：Glutaredoxins (Grxs)氧化还原蛋白质使用谷胱甘肽(γGlu-Cys-Gly;恶性疟原虫有一个经典的二硫酚(CXXC) glutaredoxin (glutaredoxin 1;三个monothiol (cxx) Grx-like蛋白质(glp),这有五个残留插入前活性部位半胱氨酸。PfGrx1已经由硫单波长反常衍射(遗憾)方法利用内在蛋白和溶剂原子。不同的构象,备用位置是精炼的活性部位Cys29由于辐射损伤。被水占据了多边形和缓冲分子。其他Grxs Grx-like蛋白质显示利用GSH-binding图案(CXXC / cxx, CDD,Lys26和Gln / Arg63)结构是守恒的。monothiol和二硫酚Grxs拥有三个守恒的水分子;位于GSH-binding网站。几个极地和带电氨基酸替换提供结构很重要额外的氢键和盐桥在其他Grxs失踪。

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