4DNX
The structure of the ATP sulfurylase from Allochromatium vinosum in the open state
Summary for 4DNX
| Entry DOI | 10.2210/pdb4dnx/pdb |
| Descriptor | Sulfate adenylyltransferase, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total) |
| Functional Keywords | rossmann-like fold, adenylsulfurylase/atp:sulfate adenylyltransferase, atp and aps, respectively, transferase |
| Biological source | Allochromatium vinosum |
| Total number of polymer chains | 2 |
| Total formula weight | 87997.45 |
| Authors | Parey, K.,Demmer, U.,Warkentin, E.,Dahl, C.,Ermler, U. (deposition date: 2012-02-09, release date: 2013-02-13, Last modification date: 2023-09-13) |
| Primary citation | Parey, K.,Demmer, U.,Warkentin, E.,Wynen, A.,Ermler, U.,Dahl, C. Structural, biochemical and genetic characterization of dissimilatory ATP sulfurylase from Allochromatium vinosum. Plos One, 8:e74707-e74707, 2013 Cited by PubMed Abstract: ATP sulfurylase (ATPS) catalyzes a key reaction in the global sulfur cycle by reversibly converting inorganic sulfate (SO4 (2-)) with ATP to adenosine 5'-phosphosulfate (APS) and pyrophosphate (PPi). In this work we report on the sat encoded dissimilatory ATP sulfurylase from the sulfur-oxidizing purple sulfur bacterium Allochromatium vinosum. In this organism, the sat gene is located in one operon and co-transcribed with the aprMBA genes for membrane-bound APS reductase. Like APS reductase, Sat is dispensible for growth on reduced sulfur compounds due to the presence of an alternate, so far unidentified sulfite-oxidizing pathway in A. vinosum. Sulfate assimilation also proceeds independently of Sat by a separate pathway involving a cysDN-encoded assimilatory ATP sulfurylase. We produced the purple bacterial sat-encoded ATP sulfurylase as a recombinant protein in E. coli, determined crucial kinetic parameters and obtained a crystal structure in an open state with a ligand-free active site. By comparison with several known structures of the ATPS-APS complex in the closed state a scenario about substrate-induced conformational changes was worked out. Despite different kinetic properties ATPS involved in sulfur-oxidizing and sulfate-reducing processes are not distinguishable on a structural level presumably due to the interference between functional and evolutionary processes. PubMed: 24073218DOI: 10.1371/journal.pone.0074707 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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