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.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Yang X,Li Y,Gao Z,Li Z,Xu J,Wang W,Dong Ydoi
10.1038/s41598-017-08834-wsubject
Has Abstractpub_date
2017-08-15 00:00:00pages
8270issue
1issn
2045-2322pii
10.1038/s41598-017-08834-wjournal_volume
7pub_type
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