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- W1966261014 abstract "Pyruvate carboxylase (PC) is a conserved metabolic enzyme with important cellular functions. We report crystallographic and cryo-electron microscopy (EM) studies of Staphylococcus aureus PC (SaPC) in complex with acetyl-CoA, an allosteric activator, and mutagenesis, biochemical, and structural studies of the biotin binding site of its carboxyltransferase (CT) domain. The disease-causing A610T mutation abolishes catalytic activity by blocking biotin binding to the CT active site, and Thr908 might play a catalytic role in the CT reaction. The crystal structure of SaPC in complex with CoA reveals a symmetrical tetramer, with one CoA molecule bound to each monomer, and cryo-EM studies confirm the symmetrical nature of the tetramer. These observations are in sharp contrast to the highly asymmetrical tetramer of Rhizobium etli PC in complex with ethyl-CoA. Our structural information suggests that acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of PC that might be catalytically more competent." @default.
- W1966261014 created "2016-06-24" @default.
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- W1966261014 date "2009-06-01" @default.
- W1966261014 modified "2023-10-16" @default.
- W1966261014 title "A Symmetrical Tetramer for S. aureus Pyruvate Carboxylase in Complex with Coenzyme A" @default.
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- W1966261014 doi "https://doi.org/10.1016/j.str.2009.04.008" @default.
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