Formylglycinamide ribonucleotide amidotransferase from Salmonella typhimurium: role of ATP complexation and the glutaminase domain in catalytic coupling

The structures of formylglycinamide ribonucleotide amidotransferase from S. typhimurium either with an unliganded glutaminase domain or in complex with an ATP analogue revealed that no major conformational changes take place upon formation of the glutamyl thioester intermediate or subsequent ATP complexation; therefore, formylglycinamide ribonucleotide binding is proposed to be the mechanism of activation of catalytic coupling in the enzyme.