6YP4

Putative adenylyl cyclase HpAC1 from Hippeastrum reveals a dominant triphophatase activity

6YP4 の概要

• エントリーDOI: 10.2210/pdb6yp4/pdb
• 分子名称: Adenylate cyclase, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: triphosphatase, plant, pppase, gtp analog, substrate complex, substrate specificity, hydrolase
• 由来する生物種: Hippeastrum hybrid cultivar
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24968.62

構造登録者

Kleinboelting, S.,Steegborn, C. (登録日: 2020-04-15, 公開日: 2020-11-04, 最終更新日: 2024-01-24)

主引用文献

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

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: 33075486
DOI: 10.1016/j.jsb.2020.107649

実験手法

X-RAY DIFFRACTION (1.94541097376 Å)