Effect of a domain-spanning disulfide on aminoacyl-tRNA synthetase activity.


Enzymes regulated by allostery undergo conformational rearrangement upon binding effector molecules. For modular proteins, a flexible interface may mediate reorientation of the protein domains and transmit binding events to activate catalysis at a distance. Aminoacyl-tRNA synthetases (aaRSs) that use tRNA anticodons as identity elements can be considered… (More)
DOI: 10.1021/bi9012275