Exploring Cooperative Domain Dynamics in Thermus thermophilus Leucyl-tRNA Synthetase Using Low-Frequency Normal Mode Calculations and Statistical Coupling Analysis.

Abstract

Leucyl-tRNA synthetases are class I synthetases that catalyze the covalent attachment of leucine to the tRNAL. The three-dimensional crystal structure of Thermus thermophilus leucyl-tRNA synthetase (TtLeuRS) demonstrates a complex modular architecture where three flexible domains [the conserved connective polypeptide 1 (CP1) domain (residues 224-417), the leucine-specific (LS) domain (residues 577-634), and the zinc-1 (ZN-1) binding domain (residues 154-189)] are inserted into the central catalytic domain. In the present work, we have investigated the collective motion of various structural elements in TtLeuRS using normal mode calculations.