5CB6
Structure of adenosine-5'-phosphosulfate kinase
Summary for 5CB6
| Entry DOI | 10.2210/pdb5cb6/pdb |
| Descriptor | Probable adenylyl-sulfate kinase, ADENOSINE-5'-PHOSPHOSULFATE, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (7 entities in total) |
| Functional Keywords | synechocystis, sulfur metabolism, enzyme, kinase, transferase |
| Biological source | Synechocystis sp. (strain PCC 6803 / Kazusa) |
| Total number of polymer chains | 6 |
| Total formula weight | 137280.47 |
| Authors | Herrmann, J.,Jez, J.M. (deposition date: 2015-06-30, release date: 2015-08-26, Last modification date: 2023-09-27) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.79 Å) |
Structure validation
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