5CB8
Crystal structure of Adenosine-5'-phosphosulfate kinase in complex with APS and sulfate
5CB8 の概要
| エントリーDOI | 10.2210/pdb5cb8/pdb |
| 分子名称 | Probable adenylyl-sulfate kinase, ADENOSINE-5'-PHOSPHOSULFATE, SULFATE ION, ... (5 entities in total) |
| 機能のキーワード | synechocystis, sulfur metabolism, kinase, transferase |
| 由来する生物種 | Synechocystis sp. (strain PCC 6803 / Kazusa) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 45102.51 |
| 構造登録者 | |
| 主引用文献 | Herrmann, J.,Nathin, D.,Lee, S.G.,Sun, T.,Jez, J.M. Recapitulating the Structural Evolution of Redox Regulation in Adenosine 5'-Phosphosulfate Kinase from Cyanobacteria to Plants. J.Biol.Chem., 290:24705-24714, 2015 Cited by PubMed Abstract: In plants, adenosine 5'-phosphosulfate (APS) kinase (APSK) is required for reproductive viability and the production of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) as a sulfur donor in specialized metabolism. Previous studies of the APSK from Arabidopsis thaliana (AtAPSK) identified a regulatory disulfide bond formed between the N-terminal domain (NTD) and a cysteine on the core scaffold. This thiol switch is unique to mosses, gymnosperms, and angiosperms. To understand the structural evolution of redox control of APSK, we investigated the redox-insensitive APSK from the cyanobacterium Synechocystis sp. PCC 6803 (SynAPSK). Crystallographic analysis of SynAPSK in complex with either APS and a non-hydrolyzable ATP analog or APS and sulfate revealed the overall structure of the enzyme, which lacks the NTD found in homologs from mosses and plants. A series of engineered SynAPSK variants reconstructed the structural evolution of the plant APSK. Biochemical analyses of SynAPSK, SynAPSK H23C mutant, SynAPSK fused to the AtAPSK NTD, and the fusion protein with the H23C mutation showed that the addition of the NTD and cysteines recapitulated thiol-based regulation. These results reveal the molecular basis for structural changes leading to the evolution of redox control of APSK in the green lineage from cyanobacteria to plants. PubMed: 26294763DOI: 10.1074/jbc.M115.679514 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.88 Å) |
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