6MRE

E. coli cysteine desulfurase SufS R92A with a cysteine persulfide intermediate

6MRE の概要

• エントリーDOI: 10.2210/pdb6mre/pdb
• 関連するPDBエントリー: 6MR2 6MR6 6MRH 6MRI
• 分子名称: Cysteine desulfurase, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• 機能のキーワード: cysteine desulfurase, sufs, persulfide, transferase
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46055.27

構造登録者

Dunkle, J.A.,Frantom, P.A. (登録日: 2018-10-12, 公開日: 2019-01-09, 最終更新日: 2023-11-15)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)