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首页> 外文期刊>Journal of Molecular Biology >EFFICIENT CATALYSIS OF DISULFIDE FORMATION DURING PROTEIN FOLDING WITH A SINGLE ACTIVE-SITE CYSTEINE
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EFFICIENT CATALYSIS OF DISULFIDE FORMATION DURING PROTEIN FOLDING WITH A SINGLE ACTIVE-SITE CYSTEINE

机译：单活性半胱氨酸折叠蛋白质过程中二硫化物形成的高效催化

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Protein disulfide isomerases (PDIs) catalyze disulfide bond formation during protein folding in vivo and are essential for viability in eukaryotic cells. They share the active-site sequence C-X-X-C that forms a catalytic disulfide. The recent finding that the EUG1 protein, a PDI-related yeast protein, with C-X-X-S sequence at its active sites can complement PDI-deficiency raised the general question of whether disulfide-isomerase activity is essential for cell viability or whether PDI variants with single active-site thiol groups can be catalytically active as disulfide isomerases. We investigated the function of the catalytic cysteine residues in DsbA, a PDI-related protein required for disulfide formation in the periplasmic space of Escherichia coli, by replacing C30 and C33 with alanine. While the mutant C30A and the double mutant CC30/33AA are inactive, C33A catalyzes disulfide-interchange reactions and oxidative renaturation of the reduced, unfolded thrombin inhibitor hirudin with close to wild-type efficiency Thus, the single active-site thiol group of C30 is sufficient for disulfide-isomerase activity of the DsbA protein. [References: 31]
机译：蛋白质二硫键异构酶（PDI）在体内蛋白质折叠过程中催化二硫键的形成，对于真核细胞中的生存力至关重要。它们共享形成催化二硫键的活性位点序列C-X-X-C。最近发现EUG1蛋白是一种与PDI相关的酵母蛋白，在其活性位点具有CXXS序列可以弥补PDI缺陷，这提出了一个普遍的问题，即二硫键异构酶活性对于细胞生存力是必不可少的，还是具有单个活性的PDI变体位硫醇基团可以作为二硫键异构酶具有催化活性。我们研究了DsbA中催化半胱氨酸残基的功能，DsbA是在大肠杆菌周质空间中形成二硫键所需的PDI相关蛋白，通过用丙氨酸替代C30和C33。尽管突变体C30A和双重突变体CC30 / 33AA处于非活性状态，但C33A催化还原的，未折叠的凝血酶抑制剂水rud素的二硫键交换反应和氧化复性，接近于野生型效率，因此，C30的单个活性位点硫醇基是足以使DsbA蛋白具有二硫键异构酶活性。 [参考：31]

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