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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structures of the dimerization domains of the Escherichia coli disulfide-bond isomerase enzymes DsbC and DsbG
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Structures of the dimerization domains of the Escherichia coli disulfide-bond isomerase enzymes DsbC and DsbG

机译：结构的二聚作用域大肠杆菌二硫键异构酶的酶DsbC和DsbG

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摘要

DsbC and DsbG are periplasmic disulfide-bond isomerases, enzymes that facilitate the folding of secreted proteins with multiple disulfide bonds by catalyzing disulfide-bond rearrangement. Both enzymes also have in vitro chaperone activity. The crystal structures of these molecules are similar and both are V-shaped homodimeric modular structures. Each dimeric molecule contains two separate C-terminal thiore-doxin-fold domains, joined by hinged helical 'stalks' to a single N-terminal dimerization domain formed from the N-terminal 67 residues of each monomer. In this work, the crystal structures of the separate DsbC and DsbG dimerization domains have been determined at resolutions of 2.0 and 1.9 angstrom, respectively. The two structures are both similar to the corresponding domains in the full-length molecules, showing that the dimerization domains fold independently of the catalytic portions of the full-length molecules. Localized structural differences between DsbC and DsbG were observed near the dimer interface and may be relevant to the different functions of the two enzymes.
机译：DsbC和DsbG周质的二硫键异构酶,酶,促进折叠与多个二硫的分泌蛋白债券通过催化二硫键重排。体外酶也有伴侣活动。分子是相似的,都是v型homodimeric模块化结构。分子中含有两个独立的c端thiore-doxin-fold域,加入了铰链螺旋“茎”一个氨基端从67年氨基形成二聚作用域每个单体的残留物。晶体结构的独立DsbC DsbG二聚作用域就下定决心2.0和1.9埃分辨率,分别。到相应的完整的域分子,表明二聚作用域折叠催化部分的独立完整的分子。DsbC差异和DsbG被观察到附近的二聚体界面和可能相关两种酶的不同的功能。

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