8VBS

E. coli cysteine desulfurase SufS bound to SufE C51A

8VBS の概要

• エントリーDOI: 10.2210/pdb8vbs/pdb
• 分子名称: Cysteine desulfurase, Cysteine desulfuration protein SufE (2 entities in total)
• 機能のキーワード: pyridoxal 5'-phosphate, cysteine desulfurase, transpersulfurase, iron-sulfur cluster, persulfide, transferase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 121000.05

構造登録者

Dunkle, J.A.,Frantom, P.A.,Gilbert, N.C. (登録日: 2023-12-12, 公開日: 2024-10-16, 最終更新日: 2024-11-27)

主引用文献

Gogar, R.K.,Chhikara, N.,Vo, M.,Gilbert, N.C.,Dunkle, J.A.,Frantom, P.A.
The structure of the SufS-SufE complex reveals interactions driving protected persulfide transfer in iron-sulfur cluster biogenesis.
J.Biol.Chem., 300:107641-107641, 2024

PubMed Abstract: Fe-S clusters are critical cofactors for redox chemistry in all organisms. The cysteine desulfurase, SufS, provides sulfur in the SUF Fe-S cluster bioassembly pathway. SufS is a dimeric, pyridoxal 5'-phosphate-dependent enzyme that uses cysteine as a substrate to generate alanine and a covalent persulfide on an active site cysteine residue. SufS enzymes are activated by an accessory transpersulfurase protein, either SufE or SufU depending on the organism, which accepts the persulfide product and delivers it to downstream partners for Fe-S assembly. Here, using Escherichia coli proteins, we present the first X-ray crystal structure of a SufS/SufE complex. There is a 1:1 stoichiometry with each monomeric unit of the EcSufS dimer bound to one EcSufE subunit, though one EcSufE is rotated ∼7° closer to the EcSufS active site. EcSufE makes clear interactions with the α16 helix of EcSufS and site-directed mutants of several α16 residues were deficient in EcSufE binding. Analysis of the EcSufE structure showed a loss of electron density at the EcSufS/EcSufE interface for a flexible loop containing the highly conserved residue R119. An R119A EcSufE variant binds EcSufS but is not active in cysteine desulfurase assays and fails to support Fe-S cluster bioassembly in vivo. S-transfer assays suggest that R119A EcSufE can receive a persulfide, suggesting the residue may function in a release mechanism. The structure of the EcSufS/EcSufE complex allows for comparison with other cysteine desulfurases to understand mechanisms of protected persulfide transfer across protein interfaces.

PubMed: 39122000
DOI: 10.1016/j.jbc.2024.107641

実験手法

X-RAY DIFFRACTION (3.31 Å)