Structural analysis of Wss1 protein from saccharomyces cerevisiae

• Main Authors: Xiaoyun Yang, Yanhua Li, Zengqiang Gao, Zongqiang Li, Jianhua Xu, Wenjia Wang, Yuhui Dong
• Format: Article
• Language: English
• Published: Nature Publishing Group 2017-08-01
• Series: Scientific Reports
• Online Access: https://doi.org/10.1038/s41598-017-08834-w

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.