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DOI | 10.2210/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 | |
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: 23913692DOI: 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) |
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