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4LW2

Structural changes during cysteine desulfurase CsdA and sulfur-acceptor CsdE interactions provide insight into the trans-persulfuration

4LW2 の概要
エントリーDOI10.2210/pdb4lw2/pdb
関連するPDBエントリー4LW4
分子名称Cysteine sulfinate desulfinase, PYRIDOXAL-5'-PHOSPHATE, GLYCEROL, ... (4 entities in total)
機能のキーワードcysteine desulfurase, csda, sufs, lyase
由来する生物種Escherichia coli
タンパク質・核酸の鎖数3
化学式量合計131686.46
構造登録者
Kim, S.,Park, S.Y. (登録日: 2013-07-26, 公開日: 2013-08-07, 最終更新日: 2023-11-08)
主引用文献Kim, S.,Park, S.
Structural changes during cysteine desulfurase CsdA and sulfur acceptor CsdE interactions provide insight into the trans-persulfuration.
J.Biol.Chem., 288:27172-27180, 2013
Cited by
PubMed Abstract: In Escherichia coli, three cysteine desulfurases (IscS, SufS, and CsdA) initiate the delivery of sulfur for various biological processes such as the biogenesis of Fe-S clusters. The sulfur generated as persulfide on a cysteine residue of cysteine desulfurases is further transferred to Fe-S scaffolds (e.g. IscU) or to intermediate cysteine-containing sulfur acceptors (e.g. TusA, SufE, and CsdE) prior to its utilization. Here, we report the structures of CsdA and the CsdA-CsdE complex, which provide insight into the sulfur transfer mediated by the trans-persulfuration reaction. Analysis of the structures indicates that the conformational flexibility of the active cysteine loop in CsdE is essential for accepting the persulfide from the cysteine of CsdA. Additionally, CsdA and CsdE invoke a different binding mode than those of previously reported cysteine desulfurase (IscS) and sulfur acceptors (TusA and IscU). Moreover, the conservation of interaction-mediating residues between CsdA/SufS and CsdE/SufE further suggests that the SufS-SufE interface likely resembles that of CsdA and CsdE.
PubMed: 23913692
DOI: 10.1074/jbc.M113.480277
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.8 Å)
構造検証レポート
Validation report summary of 4lw2
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-09に公開中

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