7C8N
Crystal structure of IscU H106A variant
7C8N の概要
| エントリーDOI | 10.2210/pdb7c8n/pdb |
| 分子名称 | Nitrogen-fixing NifU domain protein, FE2/S2 (INORGANIC) CLUSTER (3 entities in total) |
| 機能のキーワード | iron-sulfur cluster biogenesis, biosynthetic protein |
| 由来する生物種 | Methanothrix thermoacetophila |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 15373.21 |
| 構造登録者 | |
| 主引用文献 | Kunichika, K.,Nakamura, R.,Fujishiro, T.,Takahashi, Y. The Structure of the Dimeric State of IscU Harboring Two Adjacent [2Fe-2S] Clusters Provides Mechanistic Insights into Cluster Conversion to [4Fe-4S]. Biochemistry, 60:1569-1572, 2021 Cited by PubMed Abstract: IscU serves as a scaffold for the assembly of a [2Fe-2S] cluster prior to its delivery to recipient protein. It has also been proposed that on one dimer of bacterial IscU, two [2Fe-2S] clusters can be converted into a single [4Fe-4S] cluster. However, lack of structural information about the dimeric state of IscU has hindered our understanding of the underlying mechanisms. In this study, we determine the X-ray crystal structure of IscU from the thermophilic archaeon and demonstrate a dimer structure of IscU in which two [2Fe-2S] clusters are facing each other in close proximity at the dimer interface. Our structure also reveals for the first time that Asp40 serves as a fourth ligand to the [2Fe-2S] cluster with three Cys ligands in each monomer, consistent with previous spectroscopic data. We confirm by EPR spectroscopic analysis that in solution two adjacent [2Fe-2S] clusters in the wild-type dimer are converted to a [4Fe-4S] cluster via reductive coupling. Furthermore, we find that the H106A substitution abolishes the reductive conversion to the [4Fe-4S] cluster without structural alteration, suggesting that His106 is functionally involved in this process. Overall, these findings provide a structural explanation for the assembly and conversion of Fe-S clusters on IscU and highlight a dynamic process that advances via association and dissociation of the IscU dimer. PubMed: 33938220DOI: 10.1021/acs.biochem.1c00112 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.5 Å) |
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