Structural analysis of Wss1 protein from saccharomyces cerevisiae
Abstract 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 stru...
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Nature Portfolio
2017
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oai:doaj.org-article:7fb2675efc6748e98d4e1ef53b356b3a2021-12-02T15:05:28ZStructural analysis of Wss1 protein from saccharomyces cerevisiae10.1038/s41598-017-08834-w2045-2322https://doaj.org/article/7fb2675efc6748e98d4e1ef53b356b3a2017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-08834-whttps://doaj.org/toc/2045-2322Abstract 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.Xiaoyun YangYanhua LiZengqiang GaoZongqiang LiJianhua XuWenjia WangYuhui DongNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-9 (2017) |
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Medicine R Science Q Xiaoyun Yang Yanhua Li Zengqiang Gao Zongqiang Li Jianhua Xu Wenjia Wang Yuhui Dong Structural analysis of Wss1 protein from saccharomyces cerevisiae |
description |
Abstract 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. |
format |
article |
author |
Xiaoyun Yang Yanhua Li Zengqiang Gao Zongqiang Li Jianhua Xu Wenjia Wang Yuhui Dong |
author_facet |
Xiaoyun Yang Yanhua Li Zengqiang Gao Zongqiang Li Jianhua Xu Wenjia Wang Yuhui Dong |
author_sort |
Xiaoyun Yang |
title |
Structural analysis of Wss1 protein from saccharomyces cerevisiae |
title_short |
Structural analysis of Wss1 protein from saccharomyces cerevisiae |
title_full |
Structural analysis of Wss1 protein from saccharomyces cerevisiae |
title_fullStr |
Structural analysis of Wss1 protein from saccharomyces cerevisiae |
title_full_unstemmed |
Structural analysis of Wss1 protein from saccharomyces cerevisiae |
title_sort |
structural analysis of wss1 protein from saccharomyces cerevisiae |
publisher |
Nature Portfolio |
publishDate |
2017 |
url |
https://doaj.org/article/7fb2675efc6748e98d4e1ef53b356b3a |
work_keys_str_mv |
AT xiaoyunyang structuralanalysisofwss1proteinfromsaccharomycescerevisiae AT yanhuali structuralanalysisofwss1proteinfromsaccharomycescerevisiae AT zengqianggao structuralanalysisofwss1proteinfromsaccharomycescerevisiae AT zongqiangli structuralanalysisofwss1proteinfromsaccharomycescerevisiae AT jianhuaxu structuralanalysisofwss1proteinfromsaccharomycescerevisiae AT wenjiawang structuralanalysisofwss1proteinfromsaccharomycescerevisiae AT yuhuidong structuralanalysisofwss1proteinfromsaccharomycescerevisiae |
_version_ |
1718388841884155904 |