GroES co-chaperonin small-angle X-ray scattering study shows ring orifice increase in solution.
GroES consists of seven identical 10 kDa subunits and is involved in assisting protein folding as the partner of another oligomeric protein, the GroEL chaperonin. Here we studied the GroES structure in solution using small-angle X-ray scattering (SAXS). The SAXS pattern, calculated for the GroES crystal structure, was found to be different from the experimental one measured in solution. The synchronic shift in the radial direction and some turning of the protein subunits eliminate the difference and result in the increase of the hole diameter in the GroES ring-like structure from 8 A in the crystal to 21 A in solution.
Timchenko
A A
AA
Institute of Protein Research, Russian Academy of Sciences, 142292, Pushchino, Russia.
Melnik
B S
BS
Kihara
H
H
Kimura
K
K
Semisotnov
G V
GV
D018835:Chaperonin 10 / Q000737:chemistry* / Q000378:metabolism*; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry*; D008958:Models, Molecular; D008970:Molecular Weight; D020836:Protein Structure, Quaternary; D012399:Rotation; D012680:Sensitivity and Specificity; D012996:Solutions; D014961:X-Ray Diffraction
D018835:Chaperonin 10; D012996:Solutions