Small-angle X-ray studies of the quaternary structure of the lac repressor from Escherichia coli.
The quarternary structures of the lac repressor molecule from Escherichia coli and its tetrametic core, which can be derived from it by proteolytic cleavage, were studied in dilute solutions by small-angle X-ray scattering. The dimensions and general shape of the lac repressor and of the tetrameric core are reported. The core itself appears to be an elongated structure, and in the intact repressor the headpieces are located at its ends. The results ar derived from model calculations and from the following molecular parameters determined from the scattering curve and the pair distance distribution function: for lac repressor, radius of gyration 5.30 +/- 0.02 nm, radius of gyration of the cross section 2.20 +/- 0.03 nm, maximum diameter 18.0 +/- 0.5 nm, hydrated volume 329 +/- 20 nm3, relative molecular mass 149 000 +/- 15 000, for tetrameric core, radius of gyration 4.92 +/- 0.02 nm, radius of gyration of the cross section 2.24 +/- 0.03 nm, maximum diameter 16.0 +/- 0.5 nm, hydrated volume 278 +/- 15 nm3, relative molecular mass 120 000 +/- 10 000.
D004926:Escherichia coli / Q000032:analysis*; D046911:Macromolecular Substances; D011487:Protein Conformation; D012097:Repressor Proteins; D012542:Scattering, Radiation; D014157:Transcription Factors; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D012097:Repressor Proteins; D014157:Transcription Factors