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- aggregation classification "P1".
- aggregation creator person.
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- aggregation date "2008".
- aggregation format "application/pdf".
- aggregation hasFormat 633405.bibtex.
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- aggregation isPartOf urn:isbn:978-3-540-72679-1.
- aggregation language "eng".
- aggregation publisher "SPRINGER-VERLAG".
- aggregation title "Structural insights into component SoxY of the thiosulfate-oxidizing multienzyme system of Chlorobaculum thiosulfatiphilum".
- aggregation abstract "We discuss the crystal structure of component SoxY of the SoxYZ complex that is known to play a key role in the sulfur-oxidizing multienzyme system of the green sulfur bacterium Chlorobaculum thiosulfatiphilum. The protein appears to be structurally similar to a monomeric immunoglobulin-like protein that oligomerizes into a tetramer via conserved contact regions between the monomers. The tetramer is a dimer of dimers and exhibits one large hydrophobic contact region in each dimer, and two small hydrophilic interface patches between the dimers. At the tetramer interface patch, two conserved redox-active C-terminal cysteines form an intersubunit disulfide bridge. Depending on the redox state of the cysteines, the tetramer is in equilibrium with the dimers, each one of which is a candidate to covalently bind a thiosulfate molecule by means of a thiol-disulfide exchange reaction with the interprotein disulfide bonds. The significant conservation level of the interfaces, the specific interactions between the subunits in the tetramer, and the dimer-tetramer equilibrium suggest that these SoxY oligomers are biologically relevant. A possible role for these protomers in the mechanism of the Sox-system is proposed.".
- aggregation authorList BK102282.
- aggregation endPage "138".
- aggregation startPage "127".
- aggregation aggregates 665738.
- aggregation isDescribedBy 633405.
- aggregation similarTo 978-3-540-72682-1_11.
- aggregation similarTo LU-633405.