Solution X-ray scattering study on the chaperonin GroEL from Escherichia coli.
The molecular architecture of native GroEL has been studied by solution X-ray scattering. The radius of gyration for the native molecule was estimated to be 66.0 A in 50 mM Tris-HCl, 100 mM KCl at pH 7.5 and 25 degrees C. The maximum dimension was estimated to be 170 A, based on the pair distance distribution function. A cylindrical structure or two heptameric rings was found to be the best for native GroEL among structures examined by using a multi-sphere model analysis in which the radius of constituent sphere was 6 A. The results of the model analysis show that the radius of GroEL is 68.0 A and the height is 150.7 A. Unexpectedly, the central penetrating hole through GroEL was not confirmed in the best-fit structure.
Igarashi
Y
Y
Department of Biochemistry, Dokkyo University School of Medicine, Tochigi, Japan.
Kimura
K
K
Ichimura
K
K
Matsuzaki
S
S
Ikura
T
T
Kuwajima
K
K
Kihara
H
H
D018834:Chaperonin 60 / Q000737:chemistry*; D004926:Escherichia coli / Q000737:chemistry*; D008956:Models, Chemical; D011487:Protein Conformation; D012542:Scattering, Radiation; D012996:Solutions; D014965:X-Rays
D018834:Chaperonin 60; D012996:Solutions