6MRH

E. coli cysteine desulfurase SufS E96A with a cysteine persulfide intermediate

Summary for 6MRH

• Entry DOI: 10.2210/pdb6mrh/pdb
• Related: 6MR2 6MR6 6MRE 6MRI
• Descriptor: Cysteine desulfurase, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: cysteine desulfurase, sufs, persulfide, transferase
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 1
• Total formula weight: 46083.35

Authors

Dunkle, J.A.,Frantom, P.A. (deposition date: 2018-10-12, release date: 2019-01-09, Last modification date: 2023-11-15)

Primary citation

Dunkle, J.A.,Bruno, M.R.,Outten, F.W.,Frantom, P.A.
Structural Evidence for Dimer-Interface-Driven Regulation of the Type II Cysteine Desulfurase, SufS.
Biochemistry, 58:687-696, 2019

PubMed 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.

PubMed: 30571100
DOI: 10.1021/acs.biochem.8b01122

Experimental method

X-RAY DIFFRACTION (2.02 Å)