3OUR

Crystal structure of complex between EIIA and a novel pyruvate decarboxylase

3OUR の概要

• エントリーDOI: 10.2210/pdb3our/pdb
• 分子名称: UPF0255 protein VV1_0328, Phosphotransferase system IIA component (3 entities in total)
• 機能のキーワード: exhibit no hydrolase activity1, lyase-transferase complex, lyase/transferase
• 由来する生物種: Vibrio vulnificus; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 275437.85

構造登録者

Jeong, C.S.,An, Y.J.,Cha, S.S. (登録日: 2010-09-15, 公開日: 2011-06-01, 最終更新日: 2023-11-01)

主引用文献

Lee, K.J.,Jeong, C.S.,An, Y.J.,Lee, H.J.,Park, S.J.,Seok, Y.J.,Kim, P.,Lee, J.H.,Lee, K.H.,Cha, S.S.
FrsA functions as a cofactor-independent decarboxylase to control metabolic flux
Nat.Chem.Biol., 7:434-436, 2011

PubMed Abstract: The interaction between fermentation-respiration switch (FrsA) protein and glucose-specific enzyme IIA(Glc) increases glucose fermentation under oxygen-limited conditions. We show that FrsA converts pyruvate to acetaldehyde and carbon dioxide in a cofactor-independent manner and that its pyruvate decarboxylation activity is enhanced by the dephosphorylated form of IIA(Glc) (d-IIA(Glc)). Crystal structures of FrsA and its complex with d-IIA(Glc) revealed residues required for catalysis as well as the structural basis for the activation by d-IIA(Glc).

PubMed: 21623357
DOI: 10.1038/nchembio.589

実験手法

X-RAY DIFFRACTION (2.2 Å)