6YP4
Putative adenylyl cyclase HpAC1 from Hippeastrum reveals a dominant triphophatase activity
Summary for 6YP4
| Entry DOI | 10.2210/pdb6yp4/pdb |
| Descriptor | Adenylate cyclase, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | triphosphatase, plant, pppase, gtp analog, substrate complex, substrate specificity, hydrolase |
| Biological source | Hippeastrum hybrid cultivar |
| Total number of polymer chains | 1 |
| Total formula weight | 24968.62 |
| Authors | Kleinboelting, S.,Steegborn, C. (deposition date: 2020-04-15, release date: 2020-11-04, Last modification date: 2024-01-24) |
| Primary citation | Kleinboelting, S.,Miehling, J.,Steegborn, C. Crystal structure and enzymatic characterization of the putative adenylyl cyclase HpAC1 from Hippeastrum reveal dominant triphosphatase activity. J.Struct.Biol., 212:107649-107649, 2020 Cited by PubMed Abstract: HpAC1, a protein from Hippeastrum hybrid cultivars, was previously suggested to be a plant adenylyl cyclase. We describe a structural and enzymatic characterization of HpAC1. A crystal structure of HpAC1 in complex with a non-hydrolyzable GTP analog confirms a generic CYTH architecture, comprising a β-barrel with an internal substrate site. The structure reveals significant active site differences to AC proteins with CYTH fold, however, and we find that HpAC1 lacks measurable AC activity. Instead, HpAC1 has substantial triphosphatase activity, indicating this protective activity or a related activity as the protein's physiological function. PubMed: 33075486DOI: 10.1016/j.jsb.2020.107649 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.94541097376 Å) |
Structure validation
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