Structural highlights
Function
E1AQY1_9ASPA
Publication Abstract from PubMed
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 beta-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.
Crystal structure and enzymatic characterization of the putative adenylyl cyclase HpAC1 from Hippeastrum reveal dominant triphosphatase activity.,Kleinboelting S, Miehling J, Steegborn C J Struct Biol. 2020 Oct 16;212(3):107649. doi: 10.1016/j.jsb.2020.107649. PMID:33075486[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2020 Oct 16;212(3):107649. doi: 10.1016/j.jsb.2020.107649. PMID:33075486 doi:http://dx.doi.org/10.1016/j.jsb.2020.107649
