Structural analysis of Wss1 protein from saccharomyces cerevisiae.

Structural analysis of Wss1 protein from saccharomyces cerevisiae.
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酿酒酵母 Wss1 蛋白的结构分析

DOI:
10.1038/s41598-017-08834-w
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发表时间:
2017-08-15
期刊:
影响因子:
4.6
通讯作者:
Dong Y
Dong Y
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Yang X;Li Y;Gao Z;Li Z;Xu J;Wang W;Dong Y

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Wss 1是一种DNA-蛋白质交联(DPC)修复蛋白,负责降解DPC中的蛋白质组分。在这项调查中,蛋白酶结构域从酿酒酵母Wss 1(ScWss 1)的晶体结构,并与已知的晶体结构的裂殖酵母prombe Wss 1(SpWss 1)进行了比较。结果表明,锌离子附近的裂缝是Wss 1最保守的核心区域,两个同系物之间的电子表面分布差异很大。通过小角X射线散射(SAXS)进一步研究了全长ScWss 1的溶液结构,这表明该蛋白质内部含有柔性区域。最后,基于结构信息,提出了酶如何被DNA底物激活的机制。
Wss1 is a DNA-protein crosslinks (DPCs) repair protein, which is responsible for degradation of the protein components in DPCs. In this investigation, crystal structure of the protease domain from saccharomyces cerevisiae Wss1 (ScWss1) was solved and was compared with the known crystal structure of Schizosaccharomyces prombe Wss1 (SpWss1). It is found that the cleft near zinc ion to be the most conserved core region of Wss1 and that the electronic surface distributions vary greatly between the two homologs. Solution architecture of the full-length ScWss1 was further investigated by small-angle X-ray scattering (SAXS), which indicated the protein contains a flexible region inside. Finally, based on the structural information, a mechanism was proposed about how the enzyme is activated by DNA substrates.
DOI: 10.1107/s0907444999000839
发表时间: 1999-04
期刊: Acta crystallographica. Section D, Biological crystallography
影响因子: --
作者:
Terwilliger TC;Berendzen J
通讯作者: Berendzen J
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发表时间: 2001-02-01
影响因子: 6.1
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发表时间: 2010-02
期刊: Acta crystallographica. Section D, Biological crystallography
影响因子: --
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通讯作者: Zwart PH