Abstract：
:SufS is a type II cysteine desulfurase and acts as the initial step in the Suf Fe-S cluster assembly pathway. In Escherichia coli, this pathway is utilized under conditions of oxidative stress and is resistant to reactive oxygen species. Mechanistically, this means SufS must shift between protecting a covalent persulfide intermediate and making it available for transfer to the next protein partner in the pathway, SufE. Here, we report five X-ray crystal structures of SufS including a new structure of SufS containing an inward-facing persulfide intermediate on C364. Additional structures of SufS variants with substitutions at the dimer interface show changes in dimer geometry and suggest a conserved β-hairpin structure plays a role in mediating interactions with SufE. These new structures, along with previous HDX-MS and biochemical data, identify an interaction network capable of communication between active-sites of the SufS dimer coordinating the shift between desulfurase and transpersulfurase activities.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Dunkle JA,Bruno MR,Outten FW,Frantom PAdoi
10.1021/acs.biochem.8b01122subject
Has Abstractpub_date
2019-02-12 00:00:00pages
687-696issue
6eissn
0006-2960issn
1520-4995journal_volume
58pub_type
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