Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5CB8

Crystal structure of Adenosine-5'-phosphosulfate kinase in complex with APS and sulfate

5CB8 の概要
エントリーDOI10.2210/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
Herrmann, J.,Jez, J.M. (登録日: 2015-06-30, 公開日: 2015-09-02, 最終更新日: 2023-09-27)
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: 26294763
DOI: 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)
構造検証レポート
Validation report summary of 5cb8
検証レポート(詳細版)ダウンロードをダウンロード

248335

件を2026-01-28に公開中

PDB statisticsPDBj update infoContact PDBjnumon