A network of dynamically conserved residues deciphers the motions of maltose transporter.

The maltose transporter of Escherichia coli is a member of the ATP-binding cassette (ABC) transporter superfamily. The crystal structures of maltose transporter MalK have been determined for distinct conformations in the presence and absence of the ligand ATP, and other interacting proteins. Using the distinct MalK structures, normal mode analysis was performed to understand the dynamics behavior of the system. A network of dynamically important residues was obtained from the normal mode analysis and the analysis of point mutation on the normal modes. Our results suggest that the intradomain rotation occurs earlier than the interdomain rotation during the maltose-binding protein (MBP)-driven conformational changes of MalK. We inquire if protein motion and functional-driven evolutionary conservation are related. The sequence conservation of MalK was analyzed to derive a network of evolutionarily important residues. There are highly significant correlations between protein sequence and protein dynamics in many regions on the maltose transporter MalK, suggesting a link between the protein evolution and dynamics. The significant overlaps between the network of dynamically important residues and the network of evolutionarily important residues form a network of dynamically conserved residues.