3our

Crystal structure of complex between EIIA and a novel pyruvate decarboxylaseCrystal structure of complex between EIIA and a novel pyruvate decarboxylase

Structural highlights 3our is a 8 chain structure with sequence from Vibrio vulnificus CMCP6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FRSA_VIBVU Catalyzes the hydrolysis of esters (PubMed:30951551). In vitro, prefers short chain alkanoate ester as substrate. Displays highest activity towards p-nitrophenyl acetate (pNPA). Has weaker activity towards p-nitrophenyl butyrate (pNPB) (PubMed:30951551). Publication Abstract from PubMed 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). FrsA functions as a cofactor-independent decarboxylase to control metabolic flux.,Lee KJ, Jeong CS, An YJ, Lee HJ, Park SJ, Seok YJ, Kim P, Lee JH, Lee KH, Cha SS Nat Chem Biol. 2011 May 29. PMID:21623357 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphotransferase 3D structures Pyruvate decarboxylase

spinqualitylabelsall models 3our, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image