Evolutionary basis for the coupled-domain motions in Thermus thermophilus leucyl-tRNA synthetase.

ABSTRACT: Aminoacyl-tRNA synthetases are multidomain proteins that catalyze the covalent attachment of amino acids to their cognate transfer RNA. Various domains of an aminoacyl-tRNA synthetase perform their specific functions in a highly coordinated manner to maintain high accuracy in protein synthesis in cells. The coordination of their function, therefore, requires communication between domains. In this study we explored the relevance of enzyme motion in domain-domain communications. Specifically, we attempted to probe whether the communication between distantly located domains of a multidomain protein is accomplished through a coordinated movement of structural elements. We investigated the collective motion in Thermus thermophilus leucyl-tRNA synthetase by studying the low frequency normal mode

SUBMITTER: Weimer KM 

PROVIDER: S-EPMC2665063 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature