3OUR

Crystal structure of complex between EIIA and a novel pyruvate decarboxylase

Summary for 3OUR

Entry DOI	10.2210/pdb3our/pdb
Descriptor	UPF0255 protein VV1_0328, Phosphotransferase system IIA component (3 entities in total)
Functional Keywords	exhibit no hydrolase activity1, lyase-transferase complex, lyase/transferase
Biological source	Vibrio vulnificus More
Total number of polymer chains	8
Total formula weight	275437.85
Authors	Jeong, C.S.,An, Y.J.,Cha, S.S. (deposition date: 2010-09-15, release date: 2011-06-01, Last modification date: 2023-11-01)
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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation