TAILIEUCHUNG - Báo cáo khoa hoc : Substrate-induced conformational changes in Plasmodium falciparum guanosine monophosphate synthetase

GMP synthetase is a glutamine amidotransferase that incorporates ammo-nia derived from glutamine into the nucleotide xanthosine 5¢-monophos-phate (XMP) to form guanosine 5¢-monophosphate (GMP). Functional coordination of domains in glutamine amidotransferases leads to upregula | IFEBS Journal Substrate-induced conformational changes in Plasmodium falciparum guanosine monophosphate synthetase Javaid Y. Bhat Roopa Venkatachala and Hemalatha Balaram Molecular Biology and Genetics Unit JawaharlalNehru Centre for Advanced Scientific Research Bangalore India Keywords conformationalchanges domain cross-talk GMP synthetase hydrogen-deuterium exchange mass spectrometry Plasmodium falciparum Correspondence H. Balaram Molecular Biology and Genetics Unit JawaharlalNehru Centre for Advanced Scientific Research Bangalore 560064 India Fax 91 80 2208 2766 Tel 91 80 2208 2812 E-mail hb@ Present address Biocon Foundation Electronic City Bangalore 560100 India Received 23 May 2011 revised 22 July 2011 accepted 4 August 2011 doi GMP synthetase is a glutamine amidotransferase that incorporates ammonia derived from glutamine into the nucleotide xanthosine 5 -monophos-phate XMP to form guanosine 5 -monophosphate GMP . Functional coordination of domains in glutamine amidotransferases leads to upregulation of glutamine hydrolysis in the presence of acceptor substrates and is a common feature in this class of enzymes. We have shown earlier that binding of substrates to the acceptor domain of Plasmodium falciparum GMP synthetase PfGMPS leads to enhancement in both glutaminase activity and rate of glutaminase inactivation by the irreversible inhibitors acivicin and diazo-oxonorleucine Bhat JY et al. 2008 Biochem J 409 263-273 a process that must be driven by conformational alterations. In this paper through the combined use of biochemical assays optical spectroscopy and mass spectrometry we demonstrate that PfGMPS undergoes conformational transitions upon binding of substrates to the acceptor domain. Limited proteolysis and hydrogen-deuterium exchange in conjunction with mass spectrometry unveil region-specific conformational changes in the ATP XMP bound state of PfGMPS. Decreased accessibility of R294 and K428 residues to

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