3MVE

Crystal structure of a novel pyruvate decarboxylase

Summary for 3MVE

• Entry DOI: 10.2210/pdb3mve/pdb
• Descriptor: UPF0255 protein VV1_0328, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: frsa, fermentation/respiration switch protein, hydrolase activator, lyase
• Biological source: Vibrio vulnificus
• Total number of polymer chains: 2
• Total formula weight: 95248.71

Authors

Cha, S.S.,Jeong, C.S.,An, Y.J. (deposition date: 2010-05-04, release date: 2011-05-18, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)