MUTATIONAL ANALYSIS OF STRUCTURE OF YEAST ARGININE PERMIASE CAN1

. Currently, the structure and functioning of transmitters, which more than 250 members in different organisms, maintaining pH and osmosis, transport of amino acids and neurotransmitters, such as serotonin, are being intensively studied. This class of proteins is characterized by low nucleotide homology, but a similar structure. Enzymes have a cylindrical shape formed by transmembrane elements consisting of α-helices. Yeast arginine permiase Can1 can serve as a good model for studying the structure and mechanism of transport. The incorporation of arginine is proton pump dependent, thus Can1 catalyzes H+/arginine symport. Inactivation of Can1 leads to resistance to the arginine analogue canavanine. Widespread use of Can1R-mutation detection system allows selecting among several thousand mutations single missense mutations that inactivate Can1 yeast arginine permiase. At the 3D level, the large mutants are ranked res. 184 out of res. 590 of the enzyme. A stable dynamic model of permiase and charge landscape have been constructed. We selected several crucial amino acid residues, any replacement of which lead to enzyme inactivation. They are increased the list of the most significant amino acid residues involved in the transport of arginine. In the future, it is planned to continue the analysis of selected amino acid residues for a more detailed understanding of the mechanism of substrate transport.