Phenylalanyl-tRNA Synthetase from Baker'Yeast: Structural Organization of the Enzyme and Its Complex with tRNAPhe as Determined by X-Ray Small-Angle Scattering

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Abstract
The quaternary structure of the phenylalanyl-tRNA synthetase EC 6.1.1.20 and its complex with tRNAPhe was studied in dilute solutions by small angle X-ray scattering. For the free synthetase, the radius of gyration was determined as 5.5 nm, the volume 523 nm3, the maximum diameter 17.5 nm and the MW as 260,000 using an isopotential specific volume of 0.735. The overall shape could be best approximated by a flat cylinder with dimensions 18.2 nm .times. 11.5 nm .times. 4 nm; the loose structure was approximated by building up the cylinder by spheres (diameter 4.2 nm). The corresponding parameters of the enzyme tRNA complex were the following: radius of gyration 5.9 nm, volume 543 nm3, maximum diameter 21 nm and MW 290,000. These parameters suggest an 1:1 complex; thus the tRNA molecule must be attached in the extension of the longer axis. From the difference in the distance distribution functions of the free enzyme and the complex a change of conformation (contraction) of the enzyme must be assumed upon the binding of the specific tRNA.