Structural basis of the complex proteins involved in the iron-sulfur cluster biogenesis

本研究确定了铁-S团簇生物发生过程中涉及的SuFC_2-SufD_2络合物的四级结构，其中SuFC与SufD的C-末端结构域结合。通过与SuFC单体结构的比较，揭示了活性中心残基的构象变化：SuFC与SufD结合后，具有与ATP结合和水解的能力。这些发现，加上SufB-SuFC-SufD复合体的生化特征，使我们提出了一个在该复合体中Fe-S簇生物合成的模型。

In this study, the quaternary structure of the SufC_2-SufD_2 complex involved in Fe-S cluster biogenesis in which SufC is bound to the C-terminal domain of SufD was determined. Comparison with the monomeric structure of SufC revealed conformational change of the active-site residues : SufC becomes competent for ATP binding and hydrolysis upon association with SufD. These findings, together with biochemical characterization of the SufB-SufC-SufD complex, have led us to propose a model for the Fe-S cluster biosynthesis in the complex.